1zps: Difference between revisions

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-[[Image:1zps.gif|left|200px]]
-<!--
+==Crystal structure of Methanobacterium thermoautotrophicum phosphoribosyl-AMP cyclohydrolase HisI==
-The line below this paragraph, containing "STRUCTURE_1zps", creates the "Structure Box" on the page.
+<StructureSection load='1zps' size='340' side='right'caption='[[1zps]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1zps]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanothermobacter_thermautotrophicus Methanothermobacter thermautotrophicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZPS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZPS FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene></td></tr>
-{{STRUCTURE_1zps|  PDB=1zps  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1zps FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zps OCA], [https://pdbe.org/1zps PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zps RCSB], [https://www.ebi.ac.uk/pdbsum/1zps PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zps ProSAT], [https://www.topsan.org/Proteins/BSGI/1zps TOPSAN]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/HIS3_METTH HIS3_METTH] Catalyzes the hydrolysis of the adenine ring of phosphoribosyl-AMP.
+== 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/zp/1zps_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=1zps ConSurf].
+<div style="clear:both"></div>
-'''Crystal structure of Methanobacterium thermoautotrophicum phosphoribosyl-AMP cyclohydrolase HisI'''
+==See Also==
+*[[Cyclohydrolase 3D structures|Cyclohydrolase 3D structures]]
+__TOC__
-==Overview==
+</StructureSection>
-The metabolic pathway for histidine biosynthesis is interesting from an evolutionary perspective because of the diversity of gene organizations and protein structures involved. Hydrolysis of phosphoribosyl-AMP, the third step in the histidine biosynthetic pathway, is carried out by PR-AMP cyclohydrolase, the product of the hisI gene. The three-dimensional structure of PR-AMP cyclohydrolase from Methanobacterium thermoautotrophicum was solved and refined to 1.7 A resolution. The enzyme is a homodimer. The position of the Zn(2+)-binding site that is essential for catalysis was inferred from the positions of bound Cd(2+) ions, which were part of the crystallization medium. These metal binding sites include three cysteine ligands, two from one monomer and the third from the second monomer. The enzyme remains active when Cd(2+) is substituted for Zn(2+). The likely binding site for Mg(2+), also necessary for activity in a homologous cyclohydrolase, was also inferred from Cd(2+) positions and is comprised of aspartic acid side chains. The putative substrate-binding cleft is formed at the interface between the two monomers of the dimer. This fact, combined with the localization of the Zn(2+)-binding site, indicates that the enzyme is an obligate dimer.
+[[Category: Large Structures]]
-==About this Structure==
-ZPS is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Methanothermobacter_thermautotrophicus Methanothermobacter thermautotrophicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZPS OCA].
-==Reference==
-Crystal structure of Methanobacterium thermoautotrophicum phosphoribosyl-AMP cyclohydrolase HisI., Sivaraman J, Myers RS, Boju L, Sulea T, Cygler M, Jo Davisson V, Schrag JD, Biochemistry. 2005 Aug 2;44(30):10071-80. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16042384 16042384]
 [[Category: Methanothermobacter thermautotrophicus]]
-[[Category: Phosphoribosyl-AMP cyclohydrolase]]
+[[Category: Boju L]]
-[[Category: Single protein]]
+[[Category: Cygler M]]
-[[Category: BSGI, Montreal-Kingston Bacterial Structural Genomics Initiative.]]
+[[Category: Davisson VJ]]
-[[Category: Boju, L.]]
+[[Category: Myers RS]]
-[[Category: Cygler, M.]]
+[[Category: Schrag JD]]
-[[Category: Davisson, V J.]]
+[[Category: Sivaraman J]]
-[[Category: Myers, R S.]]
+[[Category: Sulea T]]
-[[Category: Schrag, J D.]]
-[[Category: Sivaraman, J.]]
-[[Category: Sulea, T.]]
-[[Category: Bsgi]]
-[[Category: Histidine biosynthesis]]
-[[Category: Montreal-kingston bacterial structural genomics initiative]]
-[[Category: Structural genomic]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 17:55:17 2008''