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| | <StructureSection load='2nxv' size='340' side='right'caption='[[2nxv]], [[Resolution|resolution]] 1.10Å' scene=''> | | <StructureSection load='2nxv' size='340' side='right'caption='[[2nxv]], [[Resolution|resolution]] 1.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2nxv]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_33485 Atcc 33485]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NXV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2NXV FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2nxv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Fuscovulum_blasticum Fuscovulum blasticum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NXV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NXV FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 1.1Å</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=2nxv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nxv OCA], [http://pdbe.org/2nxv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2nxv RCSB], [http://www.ebi.ac.uk/pdbsum/2nxv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2nxv ProSAT]</span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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=2nxv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nxv OCA], [https://pdbe.org/2nxv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2nxv RCSB], [https://www.ebi.ac.uk/pdbsum/2nxv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2nxv ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/YAT6_FUSBL YAT6_FUSBL] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 33485]] | + | [[Category: Fuscovulum blasticum]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Enroth, C]] | + | [[Category: Enroth C]] |
| - | [[Category: Strid, A]] | + | [[Category: Strid A]] |
| - | [[Category: Atpase operon]]
| + | |
| - | [[Category: Glycosyl transferase]]
| + | |
| - | [[Category: Majastridin]]
| + | |
| - | [[Category: Rossmann fold]]
| + | |
| - | [[Category: Sulphur sad]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
YAT6_FUSBL
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
The F1-ATP synthase atp operon in the proteobacterium Rhodobacter blasticus contains six open reading frames, encoding six hypothetical proteins. Five of these subunits, in the stoichiometry (alphabeta)3gamma delta epsilon make up the catalytic F1-ATP synthase complex similarly in bacteria, chloroplasts and mitochondria. The sixth gene of the R. blasticus atp operon, urf6, shows very little sequence homology to any protein of known structure or function. The gene has previously been cloned, the product (called majastridin) has been heterologously expressed in Escherichia coli, and purified to high homogeneity [M. Brosche, I. Kalbina, M. Arnfelt, G. Benito, B.G. Karlsson, A. Strid, Occurrence, overexpression and partial purification of the protein (majastridin) corresponding to the URF6 gene of the Rhodobacter blasticus atp operon, Eur. J. Biochem. 255 (1998) 87-92]. We have solved the X-ray crystal structure and refined a model of majastridin to atomic resolution. Here we present the crystal structures of apo-majastridin and the complex of majastridin with Mn2+ and UDP and show that it has extensive structural similarity to glycosyltransferases (EC 2.4). This is the first structure determined from a new group of distantly related bacterial proteins of at least six members. They share the identical amino acids that bind Mn2+ and a triplet of amino acids in the putative sugar-binding site.
Crystal structure of a protein, structurally related to glycosyltransferases, encoded in the Rhodobacter blasticus atp operon.,Enroth C, Strid A Biochim Biophys Acta. 2008 Feb;1784(2):379-84. Epub 2007 Nov 19. PMID:18067873[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Enroth C, Strid A. Crystal structure of a protein, structurally related to glycosyltransferases, encoded in the Rhodobacter blasticus atp operon. Biochim Biophys Acta. 2008 Feb;1784(2):379-84. Epub 2007 Nov 19. PMID:18067873 doi:10.1016/j.bbapap.2007.11.005
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