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| - | ==Alanine racemase from Acinetobacter baumannii==
| + | #REDIRECT [[4qhr]] This PDB entry is obsolete and replaced by 4qhr |
| - | <StructureSection load='4tlo' size='340' side='right' caption='[[4tlo]], [[Resolution|resolution]] 1.90Å' scene=''>
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| - | == Structural highlights ==
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| - | <table><tr><td colspan='2'>[[4tlo]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TLO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4TLO FirstGlance]. <br>
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| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>
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| - | <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>
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| - | <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=4tlo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tlo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4tlo RCSB], [http://www.ebi.ac.uk/pdbsum/4tlo PDBsum]</span></td></tr>
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| - | </table>
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| - | == Function ==
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| - | [[http://www.uniprot.org/uniprot/K1ER37_ACIBA K1ER37_ACIBA]] Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids (By similarity).[HAMAP-Rule:MF_01201]
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| - | <div style="background-color:#fffaf0;">
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| - | == Publication Abstract from PubMed ==
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| - | 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.
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| - | 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<ref>PMID:25195891</ref>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
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| - | == References ==
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| - | <references/>
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| - | __TOC__
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| - | </StructureSection>
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| - | [[Category: Alanine racemase]]
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| - | [[Category: Davis, E]]
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| - | [[Category: Krause, K L]]
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| - | [[Category: Scaletti, E R]]
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| - | [[Category: Alpha/beta barrel]]
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| - | [[Category: Plp]]
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