4fk9
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4fk9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_sp._SirexAA-E Streptomyces sp. SirexAA-E]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FK9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FK9 FirstGlance]. <br> | <table><tr><td colspan='2'>[[4fk9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_sp._SirexAA-E Streptomyces sp. SirexAA-E]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FK9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FK9 FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 1.06Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=4fk9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fk9 OCA], [https://pdbe.org/4fk9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fk9 RCSB], [https://www.ebi.ac.uk/pdbsum/4fk9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fk9 ProSAT]</span></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=4fk9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fk9 OCA], [https://pdbe.org/4fk9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fk9 RCSB], [https://www.ebi.ac.uk/pdbsum/4fk9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fk9 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/G2NHM6_STREK G2NHM6_STREK] | [https://www.uniprot.org/uniprot/G2NHM6_STREK G2NHM6_STREK] | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | beta-Mannanase SACTE_2347 from cellulolytic Streptomyces sp. SirexAA-E is abundantly secreted into the culture medium during growth on cellulosic materials. The enzyme is composed of domains from the glycoside hydrolase family 5 (GH5), fibronectin type-III (Fn3), and carbohydrate binding module family 2 (CBM2). After secretion, the enzyme is proteolyzed into three different, catalytically active variants with masses of 53, 42 and 34 kDa corresponding to the intact protein, loss of the CBM2 domain, or loss of both the Fn3 and CBM2 domains. The three variants had identical N-termini starting with Ala51, and the positions of specific proteolytic reactions in the linker sequences separating the three domains were identified. To conduct biochemical and structural characterizations, the natural proteolytic variants were reproduced by cloning and heterologously expressed in Escherichia coli. Each SACTE_2347 variant hydrolyzed only beta-1,4 mannosidic linkages, and also reacted with pure mannans containing partial galactosyl- and/or glucosyl substitutions. Examination of the X-ray crystal structure of the GH5 domain of SACTE_2347 suggests that two loops adjacent to the active site channel, which have differences in position and length relative to other closely related mannanases, play a role in producing the observed substrate selectivity. | ||
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| - | Biochemical properties and atomic resolution structure of a proteolytically processed beta-mannanase from cellulolytic Streptomyces sp. SirexAA-E.,Takasuka TE, Acheson JF, Bianchetti CM, Prom BM, Bergeman LF, Book AJ, Currie CR, Fox BG PLoS One. 2014 Apr 7;9(4):e94166. doi: 10.1371/journal.pone.0094166. eCollection , 2014. PMID:24710170<ref>PMID:24710170</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 4fk9" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
High Resolution Structure of the Catalytic Domain of Mannanase SActE_2347 from Streptomyces sp. SirexAA-E
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