1fbx

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[[Image:1fbx.gif|left|200px]]
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{{Seed}}
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{{STRUCTURE_1fbx| PDB=1fbx | SCENE= }}
{{STRUCTURE_1fbx| PDB=1fbx | SCENE= }}
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'''CRYSTAL STRUCTURE OF ZINC-CONTAINING E.COLI GTP CYCLOHYDROLASE I'''
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===CRYSTAL STRUCTURE OF ZINC-CONTAINING E.COLI GTP CYCLOHYDROLASE I===
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==Overview==
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The crystal structure of recombinant human GTP cyclohydrolase I was solved by Patterson search methods by using the coordinates of the Escherichia coli enzyme as a model. The human as well as bacterial enzyme were shown to contain an essential zinc ion coordinated to a His side chain and two thiol groups in each active site of the homodecameric enzymes that had escaped detection during earlier studies of the E. coli enzyme. The zinc ion is proposed to generate a hydroxyl nucleophile for attack of imidazole ring carbon atom eight of the substrate, GTP. It may also be involved in the hydrolytic release of formate from the intermediate, 2-amino-5-formylamino-6-ribosylamino-4(3H)-pyrimidinone 5'-triphosphate, and in the consecutive Amadori rearrangement of the ribosyl moiety.
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(as it appears on PubMed at http://www.pubmed.gov), where 11087827 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11087827}}
==About this Structure==
==About this Structure==
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[[Category: Allosteric enzyme]]
[[Category: Allosteric enzyme]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:08:54 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 03:01:04 2008''

Revision as of 00:01, 1 July 2008

Image:1fbx.png

Template:STRUCTURE 1fbx

CRYSTAL STRUCTURE OF ZINC-CONTAINING E.COLI GTP CYCLOHYDROLASE I

Template:ABSTRACT PUBMED 11087827

About this Structure

1FBX is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Zinc plays a key role in human and bacterial GTP cyclohydrolase I., Auerbach G, Herrmann A, Bracher A, Bader G, Gutlich M, Fischer M, Neukamm M, Garrido-Franco M, Richardson J, Nar H, Huber R, Bacher A, Proc Natl Acad Sci U S A. 2000 Dec 5;97(25):13567-72. PMID:11087827

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