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1n3s

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[[Image:1n3s.gif|left|200px]]
 
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==Biosynthesis of pteridins. Reaction mechanism of GTP cyclohydrolase I==
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The line below this paragraph, containing "STRUCTURE_1n3s", creates the "Structure Box" on the page.
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<StructureSection load='1n3s' size='340' side='right'caption='[[1n3s]], [[Resolution|resolution]] 2.55&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1n3s]] is a 10 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=1N3S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1N3S FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.55&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene></td></tr>
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{{STRUCTURE_1n3s| PDB=1n3s | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1n3s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n3s OCA], [https://pdbe.org/1n3s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1n3s RCSB], [https://www.ebi.ac.uk/pdbsum/1n3s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1n3s ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/GCH1_ECOLI GCH1_ECOLI]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/n3/1n3s_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1n3s ConSurf].
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<div style="clear:both"></div>
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'''Biosynthesis of pteridins. Reaction mechanism of GTP cyclohydrolase I'''
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==See Also==
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*[[Cyclohydrolase 3D structures|Cyclohydrolase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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GTP cyclohydrolase I catalyses the hydrolytic release of formate from GTP followed by cyclization to dihydroneopterin triphosphate. The enzymes from bacteria and animals are homodecamers containing one zinc ion per subunit. Replacement of Cys110, Cys181, His112 or His113 of the enzyme from Escherichia coli by serine affords catalytically inactive mutant proteins with reduced capacity to bind zinc. These mutant proteins are unable to convert GTP or the committed reaction intermediate, 2-amino-5-formylamino-6-(beta-ribosylamino)-4(3H)-pyrimidinone 5'-triphosphate, to dihydroneopterin triphosphate. The crystal structures of GTP complexes of the His113Ser, His112Ser and Cys181Ser mutant proteins determined at resolutions of 2.5A, 2.8A and 3.2A, respectively, revealed the conformation of substrate GTP in the active site cavity. The carboxylic group of the highly conserved residue Glu152 anchors the substrate GTP, by hydrogen bonding to N-3 and to the position 2 amino group. Several basic amino acid residues interact with the triphosphate moiety of the substrate. The structure of the His112Ser mutant in complex with an undefined mixture of nucleotides determined at a resolution of 2.1A afforded additional details of the peptide folding. Comparison between the wild-type and mutant enzyme structures indicates that the catalytically active zinc ion is directly coordinated to Cys110, Cys181 and His113. Moreover, the zinc ion is complexed to a water molecule, which is in close hydrogen bond contact to His112. In close analogy to zinc proteases, the zinc-coordinated water molecule is suggested to attack C-8 of the substrate affording a zinc-bound 8R hydrate of GTP. Opening of the hydrated imidazole ring affords a formamide derivative, which remains coordinated to zinc. The subsequent hydrolysis of the formamide motif has an absolute requirement for zinc ion catalysis. The hydrolysis of the formamide bond shows close mechanistic similarity with peptide hydrolysis by zinc proteases.
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==About this Structure==
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1N3S 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=1N3S OCA].
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==Reference==
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Biosynthesis of pteridines. Reaction mechanism of GTP cyclohydrolase I., Rebelo J, Auerbach G, Bader G, Bracher A, Nar H, Hosl C, Schramek N, Kaiser J, Bacher A, Huber R, Fischer M, J Mol Biol. 2003 Feb 14;326(2):503-16. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12559918 12559918]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: GTP cyclohydrolase I]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Auerbach G]]
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[[Category: Auerbach, G.]]
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[[Category: Bacher A]]
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[[Category: Bacher, A.]]
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[[Category: Bader G]]
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[[Category: Bader, G.]]
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[[Category: Bracher A]]
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[[Category: Bracher, A.]]
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[[Category: Fischer M]]
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[[Category: Fischer, M.]]
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[[Category: Hoesl C]]
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[[Category: Hoesl, C.]]
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[[Category: Huber R]]
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[[Category: Huber, R.]]
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[[Category: Kaiser J]]
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[[Category: Kaiser, J.]]
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[[Category: Nar H]]
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[[Category: Nar, H.]]
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[[Category: Rebelo J]]
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[[Category: Rebelo, J.]]
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[[Category: Schramek N]]
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[[Category: Schramek, N.]]
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[[Category: Biosynthesis]]
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[[Category: Crystal structure]]
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[[Category: Folic acid]]
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[[Category: Gtp cyclohydrolase i]]
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[[Category: Pteridine]]
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[[Category: Tetrahydropterin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:03:11 2008''
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Current revision

Biosynthesis of pteridins. Reaction mechanism of GTP cyclohydrolase I

PDB ID 1n3s

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