6ck0

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<table><tr><td colspan='2'>[[6ck0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_pylori_G27 Helicobacter pylori G27]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CK0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6CK0 FirstGlance]. <br>
<table><tr><td colspan='2'>[[6ck0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_pylori_G27 Helicobacter pylori G27]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CK0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6CK0 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]] 2.25&#8491;</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.25&#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=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=F5D:5-O-[(S)-({5-[(2R,3aS,4S,6aR)-2-hydroxyhexahydro-1H-thieno[3,4-d]imidazol-4-yl]pentanoyl}oxy){[(S)-hydroxy(phosphonooxy)phosphoryl]oxy}phosphoryl]adenosine'>F5D</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=F5D:[[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-[oxidanyl(phosphonooxy)phosphoryl]oxy-phosphoryl]+5-[(2~{R},6~{a}~{R})-2-oxidanyl-2,3,3~{a},4,6,6~{a}-hexahydro-1~{H}-thieno[3,4-d]imidazol-4-yl]pentanoate'>F5D</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=6ck0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ck0 OCA], [https://pdbe.org/6ck0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ck0 RCSB], [https://www.ebi.ac.uk/pdbsum/6ck0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ck0 ProSAT]</span></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=6ck0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ck0 OCA], [https://pdbe.org/6ck0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ck0 RCSB], [https://www.ebi.ac.uk/pdbsum/6ck0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ck0 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[https://www.uniprot.org/uniprot/B5Z8D8_HELPG B5Z8D8_HELPG]
[https://www.uniprot.org/uniprot/B5Z8D8_HELPG B5Z8D8_HELPG]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Helicobacter pylori, a type 1 carcinogen that causes human gastric ulcers and cancer, is a priority target of the Seattle Structural Genomics Center for Infectious Disease (SSGCID). These efforts include determining the structures of potential H. pylori therapeutic targets. Here, the purification, crystallization and X-ray structure of one such target, H. pylori biotin protein ligase (HpBPL), are reported. HpBPL catalyzes the activation of various biotin-dependent metabolic pathways, including fatty-acid synthesis, gluconeogenesis and amino-acid catabolism, and may facilitate the survival of H. pylori in the high-pH gastric mucosa. HpBPL is a prototypical bacterial biotin protein ligase, despite having less than 35% sequence identity to any reported structure in the Protein Data Bank. A biotinyl-5-ATP molecule sits in a well conserved cavity. HpBPL shares extensive tertiary-structural similarity with Mycobacterium tuberculosis biotin protein ligase (MtBPL), despite having less than 22% sequence identity. The active site of HpBPL is very similar to that of MtBPL and has the necessary residues to bind inhibitors developed for MtBPL.
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Co-crystal structure of Helicobacter pylori biotin protein ligase with biotinyl-5-ATP.,Ayanlade JP, Davis DE, Subramanian S, Dranow DM, Lorimer DD, Hammerson B, Myler PJ, Asojo OA Acta Crystallogr F Struct Biol Commun. 2025 Jan 1;81(Pt 1):11-18. doi: , 10.1107/S2053230X24012056. Epub 2025 Jan 1. PMID:39704719<ref>PMID:39704719</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6ck0" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Helicobacter pylori G27]]
[[Category: Helicobacter pylori G27]]
[[Category: Large Structures]]
[[Category: Large Structures]]

Current revision

Crystal Structure of Biotin Acetyl Coenzyme A Carboxylase Synthetase from Helicobacter pylori with bound Biotinylated ATP

PDB ID 6ck0

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