3vmv: Difference between revisions
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==Crystal structure of pectate lyase Bsp165PelA from Bacillus sp. N165== | ==Crystal structure of pectate lyase Bsp165PelA from Bacillus sp. N165== | ||
<StructureSection load='3vmv' size='340' side='right' caption='[[3vmv]], [[Resolution|resolution]] 1.54Å' scene=''> | <StructureSection load='3vmv' size='340' side='right'caption='[[3vmv]], [[Resolution|resolution]] 1.54Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3vmv]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3vmv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_sp._N16-5 Bacillus sp. N16-5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VMV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VMV FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.54Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | |||
<tr id=' | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3vmv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vmv OCA], [https://pdbe.org/3vmv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vmv RCSB], [https://www.ebi.ac.uk/pdbsum/3vmv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vmv ProSAT]</span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/D0VP31_9BACI D0VP31_9BACI] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 3vmv" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Bacillus]] | [[Category: Bacillus sp. N16-5]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Guo | [[Category: Guo RT]] | ||
[[Category: Huang | [[Category: Huang CH]] | ||
[[Category: Ko | [[Category: Ko TP]] | ||
[[Category: Liu | [[Category: Liu W]] | ||
[[Category: Ma | [[Category: Ma Y]] | ||
[[Category: Xue | [[Category: Xue Y]] | ||
[[Category: Zhang | [[Category: Zhang G]] | ||
[[Category: Zheng | [[Category: Zheng Y]] | ||
[[Category: Zhou | [[Category: Zhou C]] | ||
Latest revision as of 15:27, 8 November 2023
Crystal structure of pectate lyase Bsp165PelA from Bacillus sp. N165Crystal structure of pectate lyase Bsp165PelA from Bacillus sp. N165
Structural highlights
FunctionPublication Abstract from PubMedThe pectate lyase (Bsp165PelA) from Bacillus sp. N16-5 has great potential in industrial applications because it shows high specific activity under extremely alkaline conditions. Besides, activity measurement of Bsp165PelA does not require addition of calcium, in a way different from the other pectate lyases. Here we report crystal structures of Bsp165PelA in apo-form and in complex with trigalacturonate. The parallel beta-helix, active site residues and substrate binding cleft are similar to those in the other pectate lyases from Polysaccharide Lyase family 1. However, some of the highly conserved Ca(2+) binding residues and secondary structures are altered in Bsp165PelA, making it difficult to coordinate with Ca(2+) as in the other pectate lyases. We found Bsp165PelA forms some direct enzyme-substrate interactions instead of using Ca(2+) ions bridging in the extremely alkaline environment. Crystal structure and substrate-binding mode of a novel pectate lyase from alkaliphilic Bacillus sp. N16-5.,Zheng Y, Huang CH, Liu W, Ko TP, Xue Y, Zhou C, Guo RT, Ma Y Biochem Biophys Res Commun. 2012 Apr 6;420(2):269-74. Epub 2012 Mar 3. PMID:22414692[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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