View source for 9whb


==Crystal structure of VanH from Acinetobacter baumannii==
<StructureSection load='9whb' size='340' side='right'caption='[[9whb]], [[Resolution|resolution]] 2.39&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9whb]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Acinetobacter_baumannii Acinetobacter baumannii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9WHB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9WHB FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.39&#8491;</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=9whb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9whb OCA], [https://pdbe.org/9whb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9whb RCSB], [https://www.ebi.ac.uk/pdbsum/9whb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9whb ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A219CAG7_ACIBA A0A219CAG7_ACIBA] 
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== Publication Abstract from PubMed ==
Acinetobacter baumannii is an opportunistic pathogen increasingly associated with multidrug-resistant infections. Although vancomycin resistance is uncommon in Gram-negative bacteria, the emergence of resistant A. baumannii strains underscores the importance of elucidating the underlying mechanisms. VanH is a critical enzyme that catalyzes the NAD(P)H-dependent reduction of pyruvate to d-lactate, thereby enabling cell wall remodeling required for vancomycin resistance. Here, we report the crystal structure of VanH from A. baumannii, which forms a homodimer and exhibits a two-domain architecture comprising a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). These domains are connected by a flexible linker that permits substantial interdomain movement, likely facilitating catalytic activity. Leveraging this structural information, we performed in silico virtual screening and identified four chemical compounds predicted to interact with the interdomain pocket of VanH. Collectively, these findings provide critical structural insights into VanH and establish a framework for the rational design of inhibitors to combat vancomycin resistance.

Structure of VanH from Acinetobacter baumannii reveals domain dynamics and provides a platform for Anti-resistance drug design.,Kim JH, Kang YJ, Jin HB, Park HH Biochem Biophys Res Commun. 2026 Jan 1;794:153041. doi: , 10.1016/j.bbrc.2025.153041. Epub 2025 Nov 24. PMID:41297518<ref>PMID:41297518</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 9whb" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Acinetobacter baumannii]]
[[Category: Large Structures]]
[[Category: Kang YJ]]
[[Category: Park HH]]