Structure of the human S100A12-copper complex: implications for host-parasite defence

O V  Moroz; A A  Antson; S J  Grist; N J  Maitland; G G  Dodson; K S  Wilson; E  Lukanidin; I B  Bronstein

doi:10.1107/S0907444903004700

Structure of the human S100A12-copper complex: implications for host-parasite defence

O V Moroz, A A Antson, S J Grist, N J Maitland, G G Dodson, K S Wilson, E Lukanidin, I B Bronstein

Research output: Contribution to journal › Article › peer-review

Abstract

S100A12 is a member of the S100 family of EF-hand calcium-modulated proteins. Together with S100A8 and S100A9, it belongs to the calgranulin subfamily, i.e. it is mainly expressed in granulocytes, although there is an increasing body of evidence of expression in keratinocytes and psoriatic lesions. As well as being linked to inflammation, allergy and neuritogenesis, S100A12 is involved in host-parasite response, as are the other two calgranulins. Recent data suggest that the function of the S100-family proteins is modulated not only by calcium, but also by other metals such as zinc and copper. Previously, the structure of human S100A12 in low-calcium and high-calcium structural forms, crystallized in space groups R3 and P2(1), respectively, has been reported. Here, the structure of S100A12 in complex with copper ( space group P2(1)2(1)2; unit-cell parameters a = 70.6, b = 119.0, c = 90.2 Angstrom) refined at 2.19 Angstrom resolution is reported. Comparison of anomalous difference electron-density maps calculated with data collected with radiation of wavelengths 1.37 and 1.65 Angstrom shows that each monomer binds a single copper ion. The copper binds at an equivalent site to that at which another S100 protein, S100A7, binds zinc. The results suggest that copper binding may be essential for the functional role of S100A12 and probably the other calgranulins in the early immune response.

Original language	English
Pages (from-to)	859-867
Number of pages	9
Journal	Acta Crystallographica. Section D, Biological Crystallography
Volume	59
DOIs	https://doi.org/10.1107/S0907444903004700
Publication status	Published - May 2003

Keywords

CALCIUM-BINDING PROTEINS
HUMAN PSORIASIN S100A7
YEAST 2-HYBRID SYSTEM
CALGRANULIN-C
ZINC-BINDING
CRYSTAL-STRUCTURE
BOVINE BRAIN
IN-VIVO
FAMILY
CALPROTECTIN

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@article{f88dac4a01a44ac3813fc1e104273708,

title = "Structure of the human S100A12-copper complex: implications for host-parasite defence",

abstract = "S100A12 is a member of the S100 family of EF-hand calcium-modulated proteins. Together with S100A8 and S100A9, it belongs to the calgranulin subfamily, i.e. it is mainly expressed in granulocytes, although there is an increasing body of evidence of expression in keratinocytes and psoriatic lesions. As well as being linked to inflammation, allergy and neuritogenesis, S100A12 is involved in host-parasite response, as are the other two calgranulins. Recent data suggest that the function of the S100-family proteins is modulated not only by calcium, but also by other metals such as zinc and copper. Previously, the structure of human S100A12 in low-calcium and high-calcium structural forms, crystallized in space groups R3 and P2(1), respectively, has been reported. Here, the structure of S100A12 in complex with copper ( space group P2(1)2(1)2; unit-cell parameters a = 70.6, b = 119.0, c = 90.2 Angstrom) refined at 2.19 Angstrom resolution is reported. Comparison of anomalous difference electron-density maps calculated with data collected with radiation of wavelengths 1.37 and 1.65 Angstrom shows that each monomer binds a single copper ion. The copper binds at an equivalent site to that at which another S100 protein, S100A7, binds zinc. The results suggest that copper binding may be essential for the functional role of S100A12 and probably the other calgranulins in the early immune response.",

keywords = "CALCIUM-BINDING PROTEINS, HUMAN PSORIASIN S100A7, YEAST 2-HYBRID SYSTEM, CALGRANULIN-C, ZINC-BINDING, CRYSTAL-STRUCTURE, BOVINE BRAIN, IN-VIVO, FAMILY, CALPROTECTIN",

author = "Moroz, {O V} and Antson, {A A} and Grist, {S J} and Maitland, {N J} and Dodson, {G G} and Wilson, {K S} and E Lukanidin and Bronstein, {I B}",

year = "2003",

month = may,

doi = "10.1107/S0907444903004700",

language = "English",

volume = "59",

pages = "859--867",

journal = "Acta Crystallographica. Section D, Biological Crystallography",

issn = "0907-4449",

publisher = "International Union of Crystallography",

}

TY - JOUR

T1 - Structure of the human S100A12-copper complex: implications for host-parasite defence

AU - Moroz, O V

AU - Antson, A A

AU - Grist, S J

AU - Maitland, N J

AU - Dodson, G G

AU - Wilson, K S

AU - Lukanidin, E

AU - Bronstein, I B

PY - 2003/5

Y1 - 2003/5

N2 - S100A12 is a member of the S100 family of EF-hand calcium-modulated proteins. Together with S100A8 and S100A9, it belongs to the calgranulin subfamily, i.e. it is mainly expressed in granulocytes, although there is an increasing body of evidence of expression in keratinocytes and psoriatic lesions. As well as being linked to inflammation, allergy and neuritogenesis, S100A12 is involved in host-parasite response, as are the other two calgranulins. Recent data suggest that the function of the S100-family proteins is modulated not only by calcium, but also by other metals such as zinc and copper. Previously, the structure of human S100A12 in low-calcium and high-calcium structural forms, crystallized in space groups R3 and P2(1), respectively, has been reported. Here, the structure of S100A12 in complex with copper ( space group P2(1)2(1)2; unit-cell parameters a = 70.6, b = 119.0, c = 90.2 Angstrom) refined at 2.19 Angstrom resolution is reported. Comparison of anomalous difference electron-density maps calculated with data collected with radiation of wavelengths 1.37 and 1.65 Angstrom shows that each monomer binds a single copper ion. The copper binds at an equivalent site to that at which another S100 protein, S100A7, binds zinc. The results suggest that copper binding may be essential for the functional role of S100A12 and probably the other calgranulins in the early immune response.

AB - S100A12 is a member of the S100 family of EF-hand calcium-modulated proteins. Together with S100A8 and S100A9, it belongs to the calgranulin subfamily, i.e. it is mainly expressed in granulocytes, although there is an increasing body of evidence of expression in keratinocytes and psoriatic lesions. As well as being linked to inflammation, allergy and neuritogenesis, S100A12 is involved in host-parasite response, as are the other two calgranulins. Recent data suggest that the function of the S100-family proteins is modulated not only by calcium, but also by other metals such as zinc and copper. Previously, the structure of human S100A12 in low-calcium and high-calcium structural forms, crystallized in space groups R3 and P2(1), respectively, has been reported. Here, the structure of S100A12 in complex with copper ( space group P2(1)2(1)2; unit-cell parameters a = 70.6, b = 119.0, c = 90.2 Angstrom) refined at 2.19 Angstrom resolution is reported. Comparison of anomalous difference electron-density maps calculated with data collected with radiation of wavelengths 1.37 and 1.65 Angstrom shows that each monomer binds a single copper ion. The copper binds at an equivalent site to that at which another S100 protein, S100A7, binds zinc. The results suggest that copper binding may be essential for the functional role of S100A12 and probably the other calgranulins in the early immune response.

KW - CALCIUM-BINDING PROTEINS

KW - HUMAN PSORIASIN S100A7

KW - YEAST 2-HYBRID SYSTEM

KW - CALGRANULIN-C

KW - ZINC-BINDING

KW - CRYSTAL-STRUCTURE

KW - BOVINE BRAIN

KW - IN-VIVO

KW - FAMILY

KW - CALPROTECTIN

U2 - 10.1107/S0907444903004700

DO - 10.1107/S0907444903004700

M3 - Article

SN - 0907-4449

VL - 59

SP - 859

EP - 867

JO - Acta Crystallographica. Section D, Biological Crystallography

JF - Acta Crystallographica. Section D, Biological Crystallography

ER -