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| | <StructureSection load='4qhr' size='340' side='right'caption='[[4qhr]], [[Resolution|resolution]] 1.90Å' scene=''> | | <StructureSection load='4qhr' size='340' side='right'caption='[[4qhr]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4qhr]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Acibc Acibc]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4tlo 4tlo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QHR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QHR FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4qhr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Acinetobacter_baumannii_ACICU Acinetobacter baumannii ACICU]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4tlo 4tlo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QHR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4QHR FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ACICU_02378 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=405416 ACIBC])</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=4qhr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qhr OCA], [https://pdbe.org/4qhr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qhr RCSB], [https://www.ebi.ac.uk/pdbsum/4qhr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qhr ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alanine_racemase Alanine racemase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.1.1.1 5.1.1.1] </span></td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4qhr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qhr OCA], [http://pdbe.org/4qhr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4qhr RCSB], [http://www.ebi.ac.uk/pdbsum/4qhr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4qhr ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/B2HUA6_ACIBC B2HUA6_ACIBC]] Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids.[HAMAP-Rule:MF_01201] | + | [https://www.uniprot.org/uniprot/A0A0M3KKV7_ACIBC A0A0M3KKV7_ACIBC] Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids.[HAMAP-Rule:MF_01201] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Acibc]] | + | [[Category: Acinetobacter baumannii ACICU]] |
| - | [[Category: Alanine racemase]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Davis, E]] | + | [[Category: Davis E]] |
| - | [[Category: Krause, K L]] | + | [[Category: Krause KL]] |
| - | [[Category: Nakatani, Y]] | + | [[Category: Nakatani Y]] |
| - | [[Category: Scaletti-Hutchinson, E]] | + | [[Category: Scaletti-Hutchinson E]] |
| - | [[Category: Alpha/beta barrel]]
| + | |
| - | [[Category: Isomerase]]
| + | |
| - | [[Category: Racemization]]
| + | |
| Structural highlights
Function
A0A0M3KKV7_ACIBC Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids.[HAMAP-Rule:MF_01201]
Publication Abstract from PubMed
Acinetobacter baumannii is an opportunistic Gram-negative bacterium which is a common cause of hospital-acquired infections. Numerous antibiotic-resistant strains exist, emphasizing the need for the development of new antimicrobials. Alanine racemase (Alr) is a pyridoxal 5'-phosphate dependent enzyme that is responsible for racemization between enantiomers of alanine. As D-alanine is an essential component of the bacterial cell wall, its inhibition is lethal to prokaryotes, making it an excellent antibiotic drug target. The crystal structure of A. baumannii alanine racemase (AlrAba) from the highly antibiotic-resistant NCTC13302 strain has been solved to 1.9 A resolution. Comparison of AlrAba with alanine racemases from closely related bacteria demonstrates a conserved overall fold. The substrate entryway and active site of the enzymes were shown to be highly conserved. The structure of AlrAba will provide the template required for future structure-based drug-design studies.
The structure of alanine racemase from Acinetobacter baumannii.,Davis E, Scaletti-Hutchinson E, Opel-Reading H, Nakatani Y, Krause KL Acta Crystallogr F Struct Biol Commun. 2014 Sep 1;70(Pt 9):1199-205. doi:, 10.1107/S2053230X14017725. Epub 2014 Aug 29. PMID:25195891[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Davis E, Scaletti-Hutchinson E, Opel-Reading H, Nakatani Y, Krause KL. The structure of alanine racemase from Acinetobacter baumannii. Acta Crystallogr F Struct Biol Commun. 2014 Sep 1;70(Pt 9):1199-205. doi:, 10.1107/S2053230X14017725. Epub 2014 Aug 29. PMID:25195891 doi:http://dx.doi.org/10.1107/S2053230X14017725
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