1chm

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(New page: 200px<br /><applet load="1chm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1chm, resolution 1.9&Aring;" /> '''ENZYMATIC MECHANISM O...)
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[[Image:1chm.gif|left|200px]]<br /><applet load="1chm" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1chm, resolution 1.9&Aring;" />
 
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'''ENZYMATIC MECHANISM OF CREATINE AMIDINOHYDROLASE AS DEDUCED FROM CRYSTAL STRUCTURES'''<br />
 
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==Overview==
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==ENZYMATIC MECHANISM OF CREATINE AMIDINOHYDROLASE AS DEDUCED FROM CRYSTAL STRUCTURES==
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Crystal structures of the enzyme creatine amidinohydrolase (creatinase, EC, 3.5.3.3) with two different inhibitors, the reaction product sarcosine and, the substrate creatine, bound have been analyzed by X-ray diffraction, methods. With the inhibitor carbamoyl sarcosine, two different crystal, forms at different pH values have been determined. An enzymatic mechanism, is proposed on the basis of the eight structures analyzed. The enzyme, binds substrate and inhibitor in a distorted geometry where the urea, resonance is broken. His232 is the general base and acid, and acts as a, proton shuttle. It withdraws a proton from water 377 and donates it to the, N(3) atom of the guanidinium group. OH- 377 adds to the C(1) atom of the, guanidinium group to form a urea hydrate. Proton withdrawal by His232, leads to products. The reaction product sarcosine binds to the active site, in a reverse orientation. The free enzyme was found to have a bicarbonate, bound to the active site.
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<StructureSection load='1chm' size='340' side='right'caption='[[1chm]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1chm]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CHM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CHM FirstGlance]. <br>
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1CHM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida] with CMS as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Creatinase Creatinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.3.3 3.5.3.3] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CHM OCA].
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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]] 1.9&#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=CMS:CARBAMOYL+SARCOSINE'>CMS</scene></td></tr>
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==Reference==
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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=1chm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1chm OCA], [https://pdbe.org/1chm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1chm RCSB], [https://www.ebi.ac.uk/pdbsum/1chm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1chm ProSAT]</span></td></tr>
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Enzymatic mechanism of creatine amidinohydrolase as deduced from crystal structures., Coll M, Knof SH, Ohga Y, Messerschmidt A, Huber R, Moellering H, Russmann L, Schumacher G, J Mol Biol. 1990 Jul 20;214(2):597-610. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=1696320 1696320]
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</table>
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[[Category: Creatinase]]
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== Function ==
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[https://www.uniprot.org/uniprot/CREA_PSEPU CREA_PSEPU]
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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/ch/1chm_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=1chm ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Pseudomonas putida]]
[[Category: Pseudomonas putida]]
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[[Category: Single protein]]
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[[Category: Bartlett PA]]
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[[Category: Bartlett, P.A.]]
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[[Category: Hoeffken HW]]
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[[Category: Hoeffken, H.W.]]
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[[Category: Huber R]]
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[[Category: Huber, R.]]
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[[Category: Knof SH]]
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[[Category: Knof, S.H.]]
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[[Category: Moellering H]]
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[[Category: Moellering, H.]]
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[[Category: Schumacher G]]
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[[Category: Schumacher, G.]]
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[[Category: CMS]]
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[[Category: creatinase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:27:48 2007''
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Current revision

ENZYMATIC MECHANISM OF CREATINE AMIDINOHYDROLASE AS DEDUCED FROM CRYSTAL STRUCTURES

PDB ID 1chm

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