1fbx: Difference between revisions

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[[Image:1fbx.gif|left|200px]]<br /><applet load="1fbx" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1fbx.gif|left|200px]]
caption="1fbx, resolution 2.80&Aring;" />
 
'''CRYSTAL STRUCTURE OF ZINC-CONTAINING E.COLI GTP CYCLOHYDROLASE I'''<br />
{{Structure
|PDB= 1fbx |SIZE=350|CAPTION= <scene name='initialview01'>1fbx</scene>, resolution 2.80&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=CL:CHLORIDE ION'>CL</scene>
|ACTIVITY= [http://en.wikipedia.org/wiki/GTP_cyclohydrolase_I GTP cyclohydrolase I], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.4.16 3.5.4.16]
|GENE=
}}
 
'''CRYSTAL STRUCTURE OF ZINC-CONTAINING E.COLI GTP CYCLOHYDROLASE I'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1FBX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=CL:'>CL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/GTP_cyclohydrolase_I GTP cyclohydrolase I], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.4.16 3.5.4.16] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FBX OCA].  
1FBX is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FBX OCA].  


==Reference==
==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11087827 11087827]
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:[http://www.ncbi.nlm.nih.gov/pubmed/11087827 11087827]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: GTP cyclohydrolase I]]
[[Category: GTP cyclohydrolase I]]
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[[Category: hydrolase]]
[[Category: hydrolase]]


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Revision as of 12:07, 20 March 2008

File:1fbx.gif


PDB ID 1fbx

Drag the structure with the mouse to rotate
, resolution 2.80Å
Ligands: and
Activity: GTP cyclohydrolase I, with EC number 3.5.4.16
Coordinates: save as pdb, mmCIF, xml



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


OverviewOverview

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.

About this StructureAbout this Structure

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

ReferenceReference

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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