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1fbx

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

Structural highlights

1fbx is a 15 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.8Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

GCH1_ECOLI

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ 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. Zinc plays a key role in human and bacterial GTP cyclohydrolase I. Proc Natl Acad Sci U S A. 2000 Dec 5;97(25):13567-72. PMID:11087827 doi:10.1073/pnas.240463497

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1fbx"

@@ Line 3: / Line 3: @@
 <StructureSection load='1fbx' size='340' side='right'caption='[[1fbx]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1fbx]] is a 15 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FBX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FBX FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1fbx]] is a 15 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FBX FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1gtp|1gtp]], [[1a8r|1a8r]], [[1fb1|1fb1]]</div></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/GTP_cyclohydrolase_I GTP cyclohydrolase I], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.4.16 3.5.4.16] </span></td></tr>
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fbx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fbx OCA], [https://pdbe.org/1fbx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fbx RCSB], [https://www.ebi.ac.uk/pdbsum/1fbx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fbx ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/GCH1_ECOLI GCH1_ECOLI]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 35: / Line 36: @@
 __TOC__
 </StructureSection>
-[[Category: GTP cyclohydrolase I]]
+[[Category: Escherichia coli]]
 [[Category: Large Structures]]
-[[Category: Auerbach, G]]
+[[Category: Auerbach G]]
-[[Category: Bacher, A]]
+[[Category: Bacher A]]
-[[Category: Bader, A]]
+[[Category: Bader A]]
-[[Category: Bracher, A]]
+[[Category: Bracher A]]
-[[Category: Fischer, M]]
+[[Category: Fischer M]]
-[[Category: Garrido-Franco, M]]
+[[Category: Garrido-Franco M]]
-[[Category: Gutlich, M]]
+[[Category: Gutlich M]]
-[[Category: Herrmann, A]]
+[[Category: Herrmann A]]
-[[Category: Huber, R]]
+[[Category: Huber R]]
-[[Category: Nar, H]]
+[[Category: Nar H]]
-[[Category: Neukamm, M]]
+[[Category: Neukamm M]]
-[[Category: Richardson, J]]
+[[Category: Richardson J]]
-[[Category: Allosteric enzyme]]
-[[Category: Hydrolase]]

1fbx

From Proteopedia

Current revision

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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