View source for 3vmw


==Crystal structure of pectate lyase Bsp165PelA from Bacillus sp. N165 in complex with trigalacturonate==
<StructureSection load='3vmw' size='340' side='right'caption='[[3vmw]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3vmw]] 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=3VMW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VMW 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]] 1.9&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADA:ALPHA-D-GALACTOPYRANURONIC+ACID'>ADA</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=3vmw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vmw OCA], [https://pdbe.org/3vmw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vmw RCSB], [https://www.ebi.ac.uk/pdbsum/3vmw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vmw 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3vmw" 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]]