This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


2drw

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="2drw" size="450" color="white" frame="true" align="right" spinBox="true" caption="2drw, resolution 2.10&Aring;" /> '''The crystal structut...)
Current revision (13:48, 13 March 2024) (edit) (undo)
 
(14 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:2drw.gif|left|200px]]<br /><applet load="2drw" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="2drw, resolution 2.10&Aring;" />
 
-
'''The crystal structutre of D-amino acid amidase from Ochrobactrum anthropi SV3'''<br />
 
-
==Overview==
+
==The crystal structutre of D-amino acid amidase from Ochrobactrum anthropi SV3==
-
d-Amino acid amidase (DAA) from Ochrobactrum anthropi SV3, which catalyzes, the stereospecific hydrolysis of d-amino acid amides to yield the d-amino, acid and ammonia, has attracted increasing attention as a catalyst for the, stereospecific production of d-amino acids. In order to clarify the, structure-function relationships of DAA, the crystal structures of native, DAA, and of the d-phenylalanine/DAA complex, were determined at 2.1 and at, 2.4 A resolution, respectively. Both crystals contain six subunits (A-F), in the asymmetric unit. The fold of DAA is similar to that of the, penicillin-recognizing proteins, especially, d-alanyl-d-alanine-carboxypeptidase from Streptomyces R61, and class C, beta-lactamase from Entereobacter cloacae strain GC1. The catalytic, residues of DAA and the nucleophilic water molecule for deacylation were, assigned based on these structures. DAA has a flexible Omega-loop, similar, to class C beta-lactamase. DAA forms a pseudo acyl-enzyme intermediate, between Ser60 O(gamma) and the carbonyl moiety of d-phenylalanine in, subunits A, B, C, D, and E, but not in subunit F. The difference between, subunit F and the other subunits (A, B, C, D and E) might be attributed to, the order/disorder structure of the Omega-loop: the structure of this loop, cannot assigned in subunit F. Deacylation of subunit F may be facilitated, by the relative movement of deprotonated His307 toward Tyr149. His307, N(epsilon2) extracts the proton from Tyr149 O(eta), then Tyr149 O(eta), attacks a nucleophilic water molecule as a general base. Gln214 on the, Omega-loop is essential for forming a network of water molecules that, contains the nucleophilic water needed for deacylation. Although peptidase, activity is found in almost all penicillin-recognizing proteins, DAA lacks, peptidase activity. The lack of transpeptidase and carboxypeptidase, activities may be attributed to steric hindrance of the substrate-binding, pocket by a loop comprised of residues 278-290 and the Omega-loop.
+
<StructureSection load='2drw' size='340' side='right'caption='[[2drw]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
-
 
+
== Structural highlights ==
-
==About this Structure==
+
<table><tr><td colspan='2'>[[2drw]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Brucella_anthropi Brucella anthropi]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2d83 2d83]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DRW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DRW FirstGlance]. <br>
-
2DRW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Ochrobactrum_anthropi Ochrobactrum anthropi] with BA as [http://en.wikipedia.org/wiki/ligand ligand]. This structure superseeds the now removed PDB entry 2D83. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2DRW OCA].
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
-
 
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BA:BARIUM+ION'>BA</scene></td></tr>
-
==Reference==
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2drw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2drw OCA], [https://pdbe.org/2drw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2drw RCSB], [https://www.ebi.ac.uk/pdbsum/2drw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2drw ProSAT]</span></td></tr>
-
Crystal Structure and Functional Characterization of a D-Stereospecific Amino Acid Amidase from Ochrobactrum anthropi SV3, a New Member of the Penicillin-recognizing Proteins., Okazaki S, Suzuki A, Komeda H, Yamaguchi S, Asano Y, Yamane T, J Mol Biol. 2007 Apr 20;368(1):79-91. Epub 2006 Oct 26. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17331533 17331533]
+
</table>
-
[[Category: Ochrobactrum anthropi]]
+
== Function ==
-
[[Category: Single protein]]
+
[https://www.uniprot.org/uniprot/Q9LCC8_BRUAN Q9LCC8_BRUAN]
-
[[Category: Asano, Y.]]
+
== Evolutionary Conservation ==
-
[[Category: Komeda, H.]]
+
[[Image:Consurf_key_small.gif|200px|right]]
-
[[Category: Okazaki, S.]]
+
Check<jmol>
-
[[Category: Suzuki, A.]]
+
<jmolCheckbox>
-
[[Category: Yamane, T.]]
+
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dr/2drw_consurf.spt"</scriptWhenChecked>
-
[[Category: BA]]
+
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
-
[[Category: amidase]]
+
<text>to colour the structure by Evolutionary Conservation</text>
-
[[Category: d-stereospecific]]
+
</jmolCheckbox>
-
[[Category: hydrophobic]]
+
</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=2drw ConSurf].
-
[[Category: penicillin recognizing protein]]
+
<div style="clear:both"></div>
-
 
+
__TOC__
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 08:54:33 2007''
+
</StructureSection>
 +
[[Category: Brucella anthropi]]
 +
[[Category: Large Structures]]
 +
[[Category: Asano Y]]
 +
[[Category: Komeda H]]
 +
[[Category: Okazaki S]]
 +
[[Category: Suzuki A]]
 +
[[Category: Yamane T]]

Current revision

The crystal structutre of D-amino acid amidase from Ochrobactrum anthropi SV3

PDB ID 2drw

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools