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{{Seed}}
[[Image:3dxv.png|left|200px]]


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==The crystal structure of alpha-amino-epsilon-caprolactam racemase from Achromobacter obae==
The line below this paragraph, containing "STRUCTURE_3dxv", creates the "Structure Box" on the page.
<StructureSection load='3dxv' size='340' side='right'caption='[[3dxv]], [[Resolution|resolution]] 2.21&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'>[[3dxv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Achromobacter_obae Achromobacter obae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DXV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3DXV 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]] 2.21&#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=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>
{{STRUCTURE_3dxv|  PDB=3dxv  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3dxv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dxv OCA], [https://pdbe.org/3dxv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3dxv RCSB], [https://www.ebi.ac.uk/pdbsum/3dxv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3dxv ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ACLR_ACHOB ACLR_ACHOB] catalyzes the interconversion of L-alpha-amino-epsilon-caprolactam and D-alpha-amino-epsilon-caprolactam.<ref>PMID:19146406</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/dx/3dxv_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=3dxv ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Alpha-amino-epsilon-caprolactam (ACL) racemase (ACLR) from Achromobacter obae catalyzes the interconversion of l- and d-ACL. ACLR belongs to the fold-type I group of pyridoxal 5'-phosphate (PLP) dependent enzymes. In this study, the first crystal structures of a fold-type I racemase are solved for the native form and epsilon-caprolactam-complexed form of ACLR at 2.21 and 2.40 A resolution, respectively. Based on the location of epsilon-caprolactam in the complex structure, the substrate-binding site is assigned between Trp49 and Tyr137. The carboxyl group of Asp210 is a reasonable candidate that recognizes the nitrogen atom of a lactam or amide in the substrate. Based on a structural comparison with fold-type III alanine racemase, Tyr137 is potentially the acid/base catalytic residue that is essential for the two-base racemization mechanism. The overall structure of ACLR is similar to that of fold-type I enzymes. A structural comparison with these enzymes explains the different reaction specificities.


===The crystal structure of alpha-amino-epsilon-caprolactam racemase from Achromobacter obae===
The novel structure of a pyridoxal 5'-phosphate-dependent fold-type I racemase, alpha-amino-epsilon-caprolactam racemase from Achromobacter obae.,Okazaki S, Suzuki A, Mizushima T, Kawano T, Komeda H, Asano Y, Yamane T Biochemistry. 2009 Feb 10;48(5):941-50. PMID:19146406<ref>PMID:19146406</ref>


 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
The line below this paragraph, {{ABSTRACT_PUBMED_19146406}}, adds the Publication Abstract to the page
<div class="pdbe-citations 3dxv" style="background-color:#fffaf0;"></div>
(as it appears on PubMed at http://www.pubmed.gov), where 19146406 is the PubMed ID number.
== References ==
-->
<references/>
{{ABSTRACT_PUBMED_19146406}}
__TOC__
 
</StructureSection>
==About this Structure==
3DXV is a 2 chains structure with sequences from [http://en.wikipedia.org/wiki/Achromobacter_obae Achromobacter obae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DXV OCA].
 
==Reference==
<ref group="xtra">PMID:19146406</ref><references group="xtra"/>
[[Category: 2-aminohexano-6-lactam racemase]]
[[Category: Achromobacter obae]]
[[Category: Achromobacter obae]]
[[Category: Asano, Y.]]
[[Category: Large Structures]]
[[Category: Komeda, H.]]
[[Category: Asano Y]]
[[Category: Okazaki, S.]]
[[Category: Komeda H]]
[[Category: Suzuki, A.]]
[[Category: Okazaki S]]
[[Category: Yamane, T.]]
[[Category: Suzuki A]]
[[Category: Fold-type1]]
[[Category: Yamane T]]
[[Category: Isomerase]]
[[Category: Pyridoxal phosphate]]
[[Category: Pyridoxal-5'-phosphate dependent racemase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Sep 29 07:42:57 2010''

Latest revision as of 15:15, 1 November 2023

The crystal structure of alpha-amino-epsilon-caprolactam racemase from Achromobacter obae

3dxv, resolution 2.21Å

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