|
|
| Line 3: |
Line 3: |
| | <StructureSection load='1wzz' size='340' side='right'caption='[[1wzz]], [[Resolution|resolution]] 1.65Å' scene=''> | | <StructureSection load='1wzz' size='340' side='right'caption='[[1wzz]], [[Resolution|resolution]] 1.65Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1wzz]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"acetobacter_bordeaux"_(sic)_janke_1957 "acetobacter bordeaux" (sic) janke 1957]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WZZ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1WZZ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1wzz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Komagataeibacter_xylinus Komagataeibacter xylinus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WZZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WZZ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.65Å</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=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cmcAX ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=28448 "Acetobacter bordeaux" (sic) Janke 1957])</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=1wzz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wzz OCA], [https://pdbe.org/1wzz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wzz RCSB], [https://www.ebi.ac.uk/pdbsum/1wzz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wzz ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cellulase Cellulase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.4 3.2.1.4] </span></td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1wzz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wzz OCA], [http://pdbe.org/1wzz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1wzz RCSB], [http://www.ebi.ac.uk/pdbsum/1wzz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1wzz ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/GUNA_NOVHA GUNA_NOVHA] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Line 29: |
Line 29: |
| | </div> | | </div> |
| | <div class="pdbe-citations 1wzz" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 1wzz" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Glucanase 3D structures|Glucanase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Cellulase]] | + | [[Category: Komagataeibacter xylinus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Kawano, S]] | + | [[Category: Kawano S]] |
| - | [[Category: Munekata, M]] | + | [[Category: Munekata M]] |
| - | [[Category: Structural genomic]]
| + | [[Category: Satoh Y]] |
| - | [[Category: Satoh, Y]] | + | [[Category: Tajima K]] |
| - | [[Category: Tajima, K]] | + | [[Category: Tanaka I]] |
| - | [[Category: Tanaka, I]] | + | [[Category: Yao M]] |
| - | [[Category: Yao, M]] | + | [[Category: Yasutake Y]] |
| - | [[Category: Yasutake, Y]] | + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Sgcge]]
| + | |
| Structural highlights
Function
GUNA_NOVHA
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Previous studies have demonstrated that endoglucanase is required for cellulose biosynthesis both in bacteria and plants. However, it has yet to be elucidated how the endoglucanases function in the mechanism of cellulose biosynthesis. Here we describe the crystal structure of the cellulose biosynthesis-related endo-beta-1,47-glucanase (CMCax; EC 3.2.1.4) from the cellulose-producing Gramnegative bacterium, Acetobacter xylinum (= Gluconacetobacter xylinus), determined at 1.65-A resolution. CMCax falls into the glycoside hydrolase family 8 (GH-8), and the structure showed that the overall fold of the CMCax is similar to those of other glycoside hydrolases belonging to GH-8. Structure comparison with Clostridium thermocellum CelA, the best characterized GH-8 endoglucanase, revealed that sugar recognition subsite +3 is completely missing in CMCax. The absence of the subsite +3 leads to significant broadness of the cleft at the cellooligosaccharide reducing-end side. CMCax is known to be a secreted enzyme and is present in the culture medium. However, electron microscopic analysis using immunostaining clearly demonstrated that a portion of CMCax is localized to the cell surface, suggesting a link with other known membrane-anchored endoglucanases that are required for cellulose biosynthesis.
Structural characterization of the Acetobacter xylinum endo-beta-1,4-glucanase CMCax required for cellulose biosynthesis.,Yasutake Y, Kawano S, Tajima K, Yao M, Satoh Y, Munekata M, Tanaka I Proteins. 2006 Sep 1;64(4):1069-77. PMID:16804941[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Yasutake Y, Kawano S, Tajima K, Yao M, Satoh Y, Munekata M, Tanaka I. Structural characterization of the Acetobacter xylinum endo-beta-1,4-glucanase CMCax required for cellulose biosynthesis. Proteins. 2006 Sep 1;64(4):1069-77. PMID:16804941 doi:10.1002/prot.21052
|
