1fbx: Difference between revisions

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-[[Image:1fbx.gif|left|200px]]
-<!--
-The line below this paragraph, containing "STRUCTURE_1fbx", creates the "Structure Box" on the page.
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-or leave the SCENE parameter empty for the default display.
--->
-{{STRUCTURE_1fbx|  PDB=1fbx  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF ZINC-CONTAINING E.COLI GTP CYCLOHYDROLASE I'''
+==CRYSTAL STRUCTURE OF ZINC-CONTAINING E.COLI GTP CYCLOHYDROLASE I==
+<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 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='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='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='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]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fb/1fbx_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1fbx ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== 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.
-==Overview==
+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<ref>PMID:11087827</ref>
-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 Structure==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-FBX 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].
+</div>
+<div class="pdbe-citations 1fbx" style="background-color:#fffaf0;"></div>
-==Reference==
+==See Also==
-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]
+*[[Cyclohydrolase 3D structures|Cyclohydrolase 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Escherichia coli]]
-[[Category: GTP cyclohydrolase I]]
+[[Category: Large Structures]]
-[[Category: Single protein]]
+[[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]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 16:08:54 2008''