3vmv: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
 
(2 intermediate revisions by the same user not shown)
Line 1: Line 1:
==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]] 1.54&Aring;' scene=''>
<StructureSection load='3vmv' size='340' side='right'caption='[[3vmv]], [[Resolution|resolution]] 1.54&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3vmv]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus Bacillus]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3VMV FirstGlance]. <br>
<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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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]] 1.54&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3vmw|3vmw]]</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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GU088530, pelA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1386 Bacillus])</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>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Pectate_lyase Pectate lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.2.2 4.2.2.2] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3vmv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vmv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3vmv RCSB], [http://www.ebi.ac.uk/pdbsum/3vmv PDBsum]</span></td></tr>
</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 ==
Line 17: Line 18:
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, 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: Pectate lyase]]
[[Category: Large Structures]]
[[Category: Guo, R T]]
[[Category: Guo RT]]
[[Category: Huang, C H]]
[[Category: Huang CH]]
[[Category: Ko, T P]]
[[Category: Ko TP]]
[[Category: Liu, W]]
[[Category: Liu W]]
[[Category: Ma, Y]]
[[Category: Ma Y]]
[[Category: Xue, Y]]
[[Category: Xue Y]]
[[Category: Zhang, G]]
[[Category: Zhang G]]
[[Category: Zheng, Y]]
[[Category: Zheng Y]]
[[Category: Zhou, C]]
[[Category: Zhou C]]
[[Category: Beta-helix]]
[[Category: Lyase]]
[[Category: Pectolytic]]
[[Category: Polygalacturonate]]
[[Category: Polysaccharide lyase family 1]]

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

3vmv is a 1 chain structure with sequence from Bacillus sp. N16-5. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.54Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

D0VP31_9BACI

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Zheng Y, Huang CH, Liu W, Ko TP, Xue Y, Zhou C, Guo RT, Ma Y. Crystal structure and substrate-binding mode of a novel pectate lyase from alkaliphilic Bacillus sp. N16-5. Biochem Biophys Res Commun. 2012 Apr 6;420(2):269-74. Epub 2012 Mar 3. PMID:22414692 doi:10.1016/j.bbrc.2012.02.148

3vmv, resolution 1.54Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA