3qt9: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==Analysis of a new family of widely distributed metal-independent alpha mannosidases provides unique insight into the processing of N-linked glycans, Clostridium perfringens CPE0426 complexed with alpha-1,6-linked 1-thio-alpha-mannobiose== | ==Analysis of a new family of widely distributed metal-independent alpha mannosidases provides unique insight into the processing of N-linked glycans, Clostridium perfringens CPE0426 complexed with alpha-1,6-linked 1-thio-alpha-mannobiose== | ||
<StructureSection load='3qt9' size='340' side='right' caption='[[3qt9]], [[Resolution|resolution]] 2.05Å' scene=''> | <StructureSection load='3qt9' size='340' side='right' caption='[[3qt9]], [[Resolution|resolution]] 2.05Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3qt9]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[3qt9]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_perfringens"_veillon_and_zuber_1898 "bacillus perfringens" veillon and zuber 1898]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QT9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3QT9 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=YDR:6-S-ALPHA-D-MANNOPYRANOSYL-6-THIO-ALPHA-D-MANNOPYRANOSE'>YDR</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=YDR:6-S-ALPHA-D-MANNOPYRANOSYL-6-THIO-ALPHA-D-MANNOPYRANOSE'>YDR</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3qt3|3qt3]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3qt3|3qt3]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CPE0426 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1502 | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CPE0426 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1502 "Bacillus perfringens" Veillon and Zuber 1898])</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=3qt9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qt9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3qt9 RCSB], [http://www.ebi.ac.uk/pdbsum/3qt9 PDBsum]</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=3qt9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qt9 OCA], [http://pdbe.org/3qt9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3qt9 RCSB], [http://www.ebi.ac.uk/pdbsum/3qt9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3qt9 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
| Line 16: | Line 17: | ||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 3qt9" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Bacillus perfringens veillon and zuber 1898]] | ||
[[Category: Boraston, A B]] | [[Category: Boraston, A B]] | ||
[[Category: Deng, L E]] | [[Category: Deng, L E]] | ||
Revision as of 11:51, 5 August 2016
Analysis of a new family of widely distributed metal-independent alpha mannosidases provides unique insight into the processing of N-linked glycans, Clostridium perfringens CPE0426 complexed with alpha-1,6-linked 1-thio-alpha-mannobioseAnalysis of a new family of widely distributed metal-independent alpha mannosidases provides unique insight into the processing of N-linked glycans, Clostridium perfringens CPE0426 complexed with alpha-1,6-linked 1-thio-alpha-mannobiose
Structural highlights
Publication Abstract from PubMedThe modification of N-glycans by alpha-mannosidases is a process that is relevant to a large number of biologically important processes, including infection by microbial pathogens and colonization by microbial symbionts. At present, described mannosidases that are specific for alpha-1,6-mannose linkages are very limited in number. Through structural and functional analysis of two sequence related enzymes, one from Streptococcus pneumoniae (SpGHX) and one from Clostridium perfringens (CpGHX), a new glycoside hydrolase family, GHX, is identified and characterized. Analysis of SpGHX and CpGHX reveal them to have exo-alpha-1,6-mannosidase activity consistent with specificity for N-linked glycans having their alpha-1,3-mannose branches removed. The X-ray crystal structures of SpGHX and CpGHX obtained in apo-, inhibitor bound, and substrate bound forms provide both mechanistic and molecular insight into how these proteins, which adopt an (alpha/alpha)6-fold, recognize and hydrolyze the alpha-1,6-mannosidic bond by an inverting, metal-independent catalytic mechanism. A phylogenetic analysis of GHX proteins reveals this to be a relatively large and widespread family found frequently in bacterial pathogens, bacterial human gut symbionts, and a variety of fungi. Based on these studies we predict this family of enzymes will primarily comprise such exo-alpha-1,6-mannosidases. Analysis of new family of widely distributed metal-independent {alpha}-mannosidases provides unique insight into the processing of N-linked glycans.,Gregg KJ, Zandberg WF, Hehemann JH, Whitworth GE, Deng L, Vocadlo DJ, Boraston AB J Biol Chem. 2011 Mar 9. PMID:21388958[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||||||