The X-ray crystal structure of phosphomannose isomerase from Candida albicans at 1.7 angstrom resolution

A  Cleasby; A  Wonacott; T  Skarzynski; R E  Hubbard; G J  Davies; A E I  Proudfoot; A R  Bernard; M A  Payton; T N C  Wells

The X-ray crystal structure of phosphomannose isomerase from Candida albicans at 1.7 angstrom resolution

A Cleasby, A Wonacott, T Skarzynski, R E Hubbard, G J Davies, A E I Proudfoot, A R Bernard, M A Payton, T N C Wells

Chemistry

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

Abstract

Phosphomannose isomerase (PMI) catalyses the reversible isomerization of fructose-6-phosphate (F6P) and mannose-6-phosphate (M6P). Absence of PMI activity in yeasts causes cell lysis and thus the enzyme is a potential target for inhibition and may be a route to antifungal drugs. The 1.7 Angstrom crystal structure of PMI from Candida albicans shows that the enzyme has three distinct domains. The active site lies in the central domain, contains a single essential zinc atom, and forms a deep, open cavity of suitable dimensions to contain M6P or F6P. The central domain is flanked by a helical domain on one side and a jelly-roll like domain on the other.

Original language	English
Pages (from-to)	470-479
Number of pages	10
Journal	Nature Structural Biology
Volume	3
Issue number	5
Publication status	Published - May 1996

Keywords

SACCHAROMYCES-CEREVISIAE
PROTEIN
INTERCONVERSION
REFINEMENT
ASTACINS

Cite this

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title = "The X-ray crystal structure of phosphomannose isomerase from Candida albicans at 1.7 angstrom resolution",

abstract = "Phosphomannose isomerase (PMI) catalyses the reversible isomerization of fructose-6-phosphate (F6P) and mannose-6-phosphate (M6P). Absence of PMI activity in yeasts causes cell lysis and thus the enzyme is a potential target for inhibition and may be a route to antifungal drugs. The 1.7 Angstrom crystal structure of PMI from Candida albicans shows that the enzyme has three distinct domains. The active site lies in the central domain, contains a single essential zinc atom, and forms a deep, open cavity of suitable dimensions to contain M6P or F6P. The central domain is flanked by a helical domain on one side and a jelly-roll like domain on the other.",

keywords = "SACCHAROMYCES-CEREVISIAE, PROTEIN, INTERCONVERSION, REFINEMENT, ASTACINS",

author = "A Cleasby and A Wonacott and T Skarzynski and Hubbard, {R E} and Davies, {G J} and Proudfoot, {A E I} and Bernard, {A R} and Payton, {M A} and Wells, {T N C}",

year = "1996",

month = may,

language = "English",

volume = "3",

pages = "470--479",

journal = "Nature Structural Biology",

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TY - JOUR

T1 - The X-ray crystal structure of phosphomannose isomerase from Candida albicans at 1.7 angstrom resolution

AU - Cleasby, A

AU - Wonacott, A

AU - Skarzynski, T

AU - Hubbard, R E

AU - Davies, G J

AU - Proudfoot, A E I

AU - Bernard, A R

AU - Payton, M A

AU - Wells, T N C

PY - 1996/5

Y1 - 1996/5

N2 - Phosphomannose isomerase (PMI) catalyses the reversible isomerization of fructose-6-phosphate (F6P) and mannose-6-phosphate (M6P). Absence of PMI activity in yeasts causes cell lysis and thus the enzyme is a potential target for inhibition and may be a route to antifungal drugs. The 1.7 Angstrom crystal structure of PMI from Candida albicans shows that the enzyme has three distinct domains. The active site lies in the central domain, contains a single essential zinc atom, and forms a deep, open cavity of suitable dimensions to contain M6P or F6P. The central domain is flanked by a helical domain on one side and a jelly-roll like domain on the other.

AB - Phosphomannose isomerase (PMI) catalyses the reversible isomerization of fructose-6-phosphate (F6P) and mannose-6-phosphate (M6P). Absence of PMI activity in yeasts causes cell lysis and thus the enzyme is a potential target for inhibition and may be a route to antifungal drugs. The 1.7 Angstrom crystal structure of PMI from Candida albicans shows that the enzyme has three distinct domains. The active site lies in the central domain, contains a single essential zinc atom, and forms a deep, open cavity of suitable dimensions to contain M6P or F6P. The central domain is flanked by a helical domain on one side and a jelly-roll like domain on the other.

KW - SACCHAROMYCES-CEREVISIAE

KW - PROTEIN

KW - INTERCONVERSION

KW - REFINEMENT

KW - ASTACINS

M3 - Article

SN - 1072-8368

VL - 3

SP - 470

EP - 479

JO - Nature Structural Biology

JF - Nature Structural Biology

IS - 5

ER -