4zm6
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4zm6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhizomucor_miehei_CAU432 Rhizomucor miehei CAU432]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZM6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ZM6 FirstGlance]. <br> | <table><tr><td colspan='2'>[[4zm6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhizomucor_miehei_CAU432 Rhizomucor miehei CAU432]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZM6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ZM6 FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACO:ACETYL+COENZYME+*A'>ACO</scene>, <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]] 2.8Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACO:ACETYL+COENZYME+*A'>ACO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=4zm6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zm6 OCA], [https://pdbe.org/4zm6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4zm6 RCSB], [https://www.ebi.ac.uk/pdbsum/4zm6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4zm6 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=4zm6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zm6 OCA], [https://pdbe.org/4zm6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4zm6 RCSB], [https://www.ebi.ac.uk/pdbsum/4zm6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4zm6 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/V9M3A9_RHIMI V9M3A9_RHIMI] | [https://www.uniprot.org/uniprot/V9M3A9_RHIMI V9M3A9_RHIMI] | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Glycoside hydrolase (GH) family 3 beta-N-acetylglucosaminidases widely exist in the filamentous fungi, which may play a key role in chitin metabolism of fungi. A multi-domain GH family 3 beta-N-acetylglucosaminidase from Rhizomucor miehei (RmNag), exhibiting a potential N-acetyltransferase region, has been recently reported to show great potential in industrial applications. In this study, the crystal structure of RmNag was determined at 2.80 A resolution. The three-dimensional structure of RmNag showed four distinctive domains, which belong to two distinguishable functional regions - a GH family 3 beta-N-acetylglucosaminidase region (N-terminal) and a N-acetyltransferase region (C-terminal). From structural and functional analysis, the C-terminal region of RmNag was identified as a unique tandem array linking general control non-derepressible 5 (GCN5)-related N-acetyltransferase (GNAT), which displayed glucosamine N-acetyltransferase activity. Structural analysis of this glucosamine N-acetyltransferase region revealed that a unique glucosamine binding pocket is located in the pantetheine arm binding terminal region of the conserved CoA binding pocket, which is different from all known GNAT members. This is the first structural report of a glucosamine N-acetyltransferase, which provides novel structural information about substrate specificity of GNATs. The structural and functional features of this multi-domain beta-N-acetylglucosaminidase could be useful in studying the catalytic mechanism of GH family 3 proteins. | ||
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| - | A unique GCN5-related glucosamine N-acetyltransferase region exist in the fungal multi-domain glycoside hydrolase family 3 beta-N-acetylglucosaminidase.,Qin Z, Xiao Y, Yang X, Mesters JR, Yang S, Jiang Z Sci Rep. 2015 Dec 16;5:18292. doi: 10.1038/srep18292. PMID:26669854<ref>PMID:26669854</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 4zm6" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
A unique GCN5-related glucosamine N-acetyltransferase region exist in the fungal multi-domain GH3 beta-N-acetylglucosaminidase
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Categories: Large Structures | Rhizomucor miehei CAU432 | Jiang Z | Mesters JR | Qin Z | Xiao Y | Yang S | Yang X
