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[[Image:1chm.gif|left|200px]]


{{Structure
==ENZYMATIC MECHANISM OF CREATINE AMIDINOHYDROLASE AS DEDUCED FROM CRYSTAL STRUCTURES==
|PDB= 1chm |SIZE=350|CAPTION= <scene name='initialview01'>1chm</scene>, resolution 1.9&Aring;
<StructureSection load='1chm' size='340' side='right'caption='[[1chm]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=CMS:CARBAMOYL SARCOSINE'>CMS</scene>
<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>
|ACTIVITY= [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]
</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>
|GENE=  
<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>
}}
<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>
 
</table>
'''ENZYMATIC MECHANISM OF CREATINE AMIDINOHYDROLASE AS DEDUCED FROM CRYSTAL STRUCTURES'''
== Function ==
 
[https://www.uniprot.org/uniprot/CREA_PSEPU CREA_PSEPU]
 
== Evolutionary Conservation ==
==Overview==
[[Image:Consurf_key_small.gif|200px|right]]
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.
Check<jmol>
 
  <jmolCheckbox>
==About this Structure==
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ch/1chm_consurf.spt"</scriptWhenChecked>
1CHM is a [[Single protein]] structure of sequence from [http://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].  
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 
    <text>to colour the structure by Evolutionary Conservation</text>
==Reference==
  </jmolCheckbox>
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://www.ncbi.nlm.nih.gov/pubmed/1696320 1696320]
</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].
[[Category: Creatinase]]
<div style="clear:both"></div>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudomonas putida]]
[[Category: Pseudomonas putida]]
[[Category: Single protein]]
[[Category: Bartlett PA]]
[[Category: Bartlett, P A.]]
[[Category: Hoeffken HW]]
[[Category: Hoeffken, H W.]]
[[Category: Huber R]]
[[Category: Huber, R.]]
[[Category: Knof SH]]
[[Category: Knof, S H.]]
[[Category: Moellering H]]
[[Category: Moellering, H.]]
[[Category: Schumacher G]]
[[Category: Schumacher, G.]]
[[Category: CMS]]
[[Category: creatinase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:24:31 2008''

Latest revision as of 09:43, 7 February 2024

ENZYMATIC MECHANISM OF CREATINE AMIDINOHYDROLASE AS DEDUCED FROM CRYSTAL STRUCTURESENZYMATIC MECHANISM OF CREATINE AMIDINOHYDROLASE AS DEDUCED FROM CRYSTAL STRUCTURES

Structural highlights

1chm is a 2 chain structure with sequence from Pseudomonas putida. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.9Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CREA_PSEPU

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

1chm, resolution 1.90Å

Drag the structure with the mouse to rotate

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OCA
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