|
|
| Line 3: |
Line 3: |
| | <StructureSection load='6mgj' size='340' side='right'caption='[[6mgj]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='6mgj' size='340' side='right'caption='[[6mgj]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6mgj]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_baa-93 Atcc baa-93]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MGJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6MGJ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6mgj]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Paenibacillus_odorifer Paenibacillus odorifer]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MGJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6MGJ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PE3:3,6,9,12,15,18,21,24,27,30,33,36,39-TRIDECAOXAHENTETRACONTANE-1,41-DIOL'>PE3</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]] 2Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=PE3:3,6,9,12,15,18,21,24,27,30,33,36,39-TRIDECAOXAHENTETRACONTANE-1,41-DIOL'>PE3</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6mgl|6mgl]], [[6mgk|6mgk]]</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=6mgj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mgj OCA], [https://pdbe.org/6mgj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6mgj RCSB], [https://www.ebi.ac.uk/pdbsum/6mgj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6mgj ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BSK60_29080 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=189426 ATCC BAA-93])</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=6mgj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mgj OCA], [http://pdbe.org/6mgj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6mgj RCSB], [http://www.ebi.ac.uk/pdbsum/6mgj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6mgj ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A0A1R0YRH0_9BACL A0A1R0YRH0_9BACL] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 23: |
Line 23: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc baa-93]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Arnal, G]] | + | [[Category: Paenibacillus odorifer]] |
| - | [[Category: Brumer, H]] | + | [[Category: Arnal G]] |
| - | [[Category: Nocek, B]] | + | [[Category: Brumer H]] |
| - | [[Category: Savchenko, A]] | + | [[Category: Nocek B]] |
| - | [[Category: Skarina, T]] | + | [[Category: Savchenko A]] |
| - | [[Category: Stogios, P J]] | + | [[Category: Skarina T]] |
| - | [[Category: Family gh74]]
| + | [[Category: Stogios PJ]] |
| - | [[Category: Glycosylhydrolase]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Xyloglucanase]]
| + | |
| Structural highlights
6mgj is a 8 chain structure with sequence from Paenibacillus odorifer. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 2Å |
| Ligands: | , , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
A0A1R0YRH0_9BACL
Publication Abstract from PubMed
Paenibacillus odorifer produces a single multimodular enzyme containing a glycoside hydrolase (GH) family 74 module (AIQ73809). Recombinant production and characterization of the GH74 module (PoGH74cat) revealed a highly specific, processive endo-xyloglucanase that can hydrolyze the polysaccharide backbone at both branched and unbranched positions. X-ray crystal structures obtained for the free enzyme and oligosaccharide complexes evidenced an extensive hydrophobic binding platform - the first in GH74 extending from subsites -4 to +6 - and unique mobile active-site loops. Site-directed mutagenesis revealed that glycine-476 was uniquely responsible for the promiscuous backbone-cleaving activity of PoGH74cat; replacement with tyrosine, which is conserved in many GH74 members, resulted in exclusive hydrolysis at unbranched glucose units. Likewise, systematic replacement of the hydrophobic platform residues constituting the positive subsites indicated their relative contributions to the processive mode of action. Specifically, W347 (+3 subsite) and W348 (+5 subsite) are essential for processivity, while W406 (+2 subsite) and Y372 (+6 subsite) are not strictly essential, but aid processivity.
Structural enzymology reveals the molecular basis of substrate regiospecificity and processivity of an exemplar bacterial glycoside hydrolase family 74 endo-xyloglucanase.,Arnal G, Stogios PJ, Asohan J, Skarina T, Savchenko A, Brumer H Biochem J. 2018 Dec 19;475(24):3963-3978. doi: 10.1042/BCJ20180763. PMID:30463871[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Arnal G, Stogios PJ, Asohan J, Skarina T, Savchenko A, Brumer H. Structural enzymology reveals the molecular basis of substrate regiospecificity and processivity of an exemplar bacterial glycoside hydrolase family 74 endo-xyloglucanase. Biochem J. 2018 Dec 19;475(24):3963-3978. doi: 10.1042/BCJ20180763. PMID:30463871 doi:http://dx.doi.org/10.1042/BCJ20180763
|
