3u37: Difference between revisions
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==An Acetyl Xylan Esterase (Est2A) from the Rumen Bacterium Butyrivibrio proteoclasticus.== | |||
<StructureSection load='3u37' size='340' side='right' caption='[[3u37]], [[Resolution|resolution]] 2.10Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3u37]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Butyrivibrio_proteoclasticus_b316 Butyrivibrio proteoclasticus b316]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3U37 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3U37 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">est2A, bpr_I2939 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=515622 Butyrivibrio proteoclasticus B316])</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=3u37 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u37 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3u37 RCSB], [http://www.ebi.ac.uk/pdbsum/3u37 PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Butyrivibrio proteoclasticus is a significant component of the microbial population of the rumen of dairy cattle. It is a xylan-degrading organism whose genome encodes a large number of open reading frames annotated as fibre-degrading enzymes. We have determined the three-dimensional structure of Est2A, an acetyl xylan esterase from B. proteoclasticus, at 2.1 A resolution, along with the structure of an inactive mutant (H351A) at 2.0 A resolution. The structure reveals two domains - a C-terminal SGNH domain and an N-terminal jelly-roll domain typical of CE2 family structures. The structures are accompanied by experimentally determined enzymatic parameters against two model substrates, para-nitrophenyl acetate and para-nitrophenyl butyrate. The suite of fibre-degrading enzymes produced by B. proteoclasticus provides a rich source of new enzymes of potential use in industrial settings. Proteins 2013. (c) 2013 Wiley Periodicals, Inc. | |||
Structure and function of an acetyl xylan esterase (est2a) from the rumen bacterium Butyrivibrio proteoclasticus.,Till M, Goldstone DC, Attwood GT, Moon CD, Kelly WJ, Arcus VL Proteins. 2013 Jan 23. doi: 10.1002/prot.24254. PMID:23345031<ref>PMID:23345031</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Butyrivibrio proteoclasticus b316]] | [[Category: Butyrivibrio proteoclasticus b316]] | ||
[[Category: Arcus, V | [[Category: Arcus, V]] | ||
[[Category: Till, M | [[Category: Till, M]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
Revision as of 13:58, 20 January 2015
An Acetyl Xylan Esterase (Est2A) from the Rumen Bacterium Butyrivibrio proteoclasticus.An Acetyl Xylan Esterase (Est2A) from the Rumen Bacterium Butyrivibrio proteoclasticus.
Structural highlights
Publication Abstract from PubMedButyrivibrio proteoclasticus is a significant component of the microbial population of the rumen of dairy cattle. It is a xylan-degrading organism whose genome encodes a large number of open reading frames annotated as fibre-degrading enzymes. We have determined the three-dimensional structure of Est2A, an acetyl xylan esterase from B. proteoclasticus, at 2.1 A resolution, along with the structure of an inactive mutant (H351A) at 2.0 A resolution. The structure reveals two domains - a C-terminal SGNH domain and an N-terminal jelly-roll domain typical of CE2 family structures. The structures are accompanied by experimentally determined enzymatic parameters against two model substrates, para-nitrophenyl acetate and para-nitrophenyl butyrate. The suite of fibre-degrading enzymes produced by B. proteoclasticus provides a rich source of new enzymes of potential use in industrial settings. Proteins 2013. (c) 2013 Wiley Periodicals, Inc. Structure and function of an acetyl xylan esterase (est2a) from the rumen bacterium Butyrivibrio proteoclasticus.,Till M, Goldstone DC, Attwood GT, Moon CD, Kelly WJ, Arcus VL Proteins. 2013 Jan 23. doi: 10.1002/prot.24254. PMID:23345031[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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