2bz0: Difference between revisions

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-[[Image:2bz0.png|left|200px]]
-{{STRUCTURE_2bz0|  PDB=2bz0  |  SCENE=  }}
+==Crystal Structure of E. coli GTP cyclohydrolase II in complex with GTP analogue, GMPcPP, and Zinc==
+<StructureSection load='2bz0' size='340' side='right'caption='[[2bz0]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2bz0]] is a 2 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=2BZ0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BZ0 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]] 2.6&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=G2P:PHOSPHOMETHYLPHOSPHONIC+ACID+GUANYLATE+ESTER'>G2P</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=2bz0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bz0 OCA], [https://pdbe.org/2bz0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bz0 RCSB], [https://www.ebi.ac.uk/pdbsum/2bz0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bz0 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/RIBA_ECOLI RIBA_ECOLI] Catalyzes the conversion of GTP to 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and pyrophosphate.<ref>PMID:235552</ref>
+== 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/bz/2bz0_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=2bz0 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+GTP cyclohydrolase II converts GTP to 2,5-diamino-6-beta-ribosyl-4(3H)-pyrimidinone 5'-phosphate, formate and pyrophosphate, the first step in riboflavin biosynthesis. The essential role of riboflavin in metabolism and the absence of GTP cyclohydrolase II in higher eukaryotes makes it a potential novel selective antimicrobial drug target. GTP cyclohydrolase II catalyzes a distinctive overall reaction from GTP cyclohydrolase I; the latter converts GTP to dihydroneopterin triphosphate, utilized in folate and tetrahydrobiopterin biosynthesis. The structure of GTP cyclohydrolase II determined at 1.54-A resolution reveals both a different protein fold to GTP cyclohydrolase I and distinctive molecular recognition determinants for GTP; although in both enzymes there is a bound catalytic zinc. The GTP cyclohydrolase II.GMPCPP complex structure shows Arg(128) interacting with the alpha-phosphonate, and thus in the case of GTP, Arg(128) is positioned to act as the nucleophile for pyrophosphate release and formation of the proposed covalent guanylyl-GTP cyclohydrolase II intermediate. Tyr(105) is identified as playing a key role in GTP ring opening; it is hydrogen-bonded to the zinc-activated water molecule, the latter being positioned for nucleophilic attack on the guanine C-8 atom. Although GTP cyclohydrolase I and GTP cyclohydrolase II both use a zinc ion for the GTP ring opening and formate release, different residues are utilized in each case to catalyze this reaction step.
-===CRYSTAL STRUCTURE OF E. COLI GTP CYCLOHYDROLASE II IN COMPLEX WITH GTP ANALOGUE, GMPCPP, AND ZINC===
+GTP cyclohydrolase II structure and mechanism.,Ren J, Kotaka M, Lockyer M, Lamb HK, Hawkins AR, Stammers DK J Biol Chem. 2005 Nov 4;280(44):36912-9. Epub 2005 Aug 22. PMID:16115872<ref>PMID:16115872</ref>
-{{ABSTRACT_PUBMED_16115872}}
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2bz0" style="background-color:#fffaf0;"></div>
-==About this Structure==
+==See Also==
-[[2bz0]] is a 2 chain structure with 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=2BZ0 OCA].
+*[[Cyclohydrolase 3D structures|Cyclohydrolase 3D structures]]
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:016115872</ref><references group="xtra"/>
+__TOC__
+</StructureSection>
 [[Category: Escherichia coli]]
-[[Category: GTP cyclohydrolase II]]
+[[Category: Large Structures]]
-[[Category: Hawkins, A R.]]
+[[Category: Hawkins AR]]
-[[Category: Kotaka, M.]]
+[[Category: Kotaka M]]
-[[Category: Lamb, H K.]]
+[[Category: Lamb HK]]
-[[Category: Lockyer, M.]]
+[[Category: Lockyer M]]
-[[Category: Ren, J.]]
+[[Category: Ren J]]
-[[Category: Stammers, D K.]]
+[[Category: Stammers DK]]
-[[Category: Catalytic zinc]]
-[[Category: Gtp]]
-[[Category: Gtp cyclohydrolase ii]]
-[[Category: Hydrolase]]
-[[Category: Magnesium]]
-[[Category: Riboflavin biosynthesis]]