3vmv: Difference between revisions
New page: '''Unreleased structure''' The entry 3vmv is ON HOLD Authors: Zheng, Y., Huang, C.H., Liu, W., Ko, T.P., Xue, Y., Zhou, C., Zhang, G., Guo, R.T., Ma, Y. Description: Crystal structure ... |
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==Crystal structure of pectate lyase Bsp165PelA from Bacillus sp. N165== | |||
<StructureSection load='3vmv' size='340' side='right'caption='[[3vmv]], [[Resolution|resolution]] 1.54Å' scene=''> | |||
== Structural highlights == | |||
<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='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='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> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/D0VP31_9BACI D0VP31_9BACI] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The 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<ref>PMID:22414692</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3vmv" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bacillus sp. N16-5]] | |||
[[Category: Large Structures]] | |||
[[Category: Guo RT]] | |||
[[Category: Huang CH]] | |||
[[Category: Ko TP]] | |||
[[Category: Liu W]] | |||
[[Category: Ma Y]] | |||
[[Category: Xue Y]] | |||
[[Category: Zhang G]] | |||
[[Category: Zheng Y]] | |||
[[Category: Zhou C]] | |||