View source for 5cvy


==The Structure of Bacillus pumilus GH48 in complex with cellobiose and cellohexaose==
<StructureSection load='5cvy' size='340' side='right'caption='[[5cvy]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5cvy]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_pumilus_SAFR-032 Bacillus pumilus SAFR-032]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CVY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CVY 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&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PRD_900005:beta-cellobiose'>PRD_900005</scene>, <scene name='pdbligand=PRD_900020:beta-cellohexaose'>PRD_900020</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=5cvy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cvy OCA], [https://pdbe.org/5cvy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cvy RCSB], [https://www.ebi.ac.uk/pdbsum/5cvy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cvy ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A8FDC4_BACP2 A8FDC4_BACP2] 
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== Publication Abstract from PubMed ==
Glycoside hydrolase (GH) family 48 is an understudied and increasingly important exoglucanase family found in the majority of bacterial cellulase systems. Moreover, many thermophilic enzyme systems contain GH48 enzymes. Deletion of GH48 enzymes in these microorganisms results in drastic reduction in biomass deconstruction. Surprisingly, given their importance for these microorganisms, GH48s have intrinsically low cellulolytic activity but even in low ratios synergize greatly with GH9 endoglucanases. In this study, we explore the structural and enzymatic diversity of these enzymes across a wide range of temperature optima. We have crystallized one new GH48 module from Bacillus pumilus in a complex with cellobiose and cellohexaose (BpumGH48). We compare this structure to other known GH48 enzymes in an attempt to understand GH48 structure/function relationships and draw general rules correlating amino acid sequences and secondary structures to thermostability in this GH family.

Natural diversity of glycoside hydrolase family 48 exoglucanases: insights from structure.,Brunecky R, Alahuhta M, Sammond DW, Xu Q, Chen M, Wilson DB, Brady JW, Himmel ME, Bomble YJ, Lunin VV Biotechnol Biofuels. 2017 Nov 30;10:274. doi: 10.1186/s13068-017-0951-5., eCollection 2017. PMID:29213319<ref>PMID:29213319</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5cvy" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Bacillus pumilus SAFR-032]]
[[Category: Large Structures]]
[[Category: Alahuhta PM]]
[[Category: Lunin VV]]