2hhc
From Proteopedia
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<StructureSection load='2hhc' size='340' side='right'caption='[[2hhc]], [[Resolution|resolution]] 1.54Å' scene=''> | <StructureSection load='2hhc' size='340' side='right'caption='[[2hhc]], [[Resolution|resolution]] 1.54Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2hhc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[2hhc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bradyrhizobium_sp._WM9 Bradyrhizobium sp. WM9]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HHC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HHC FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.54Å</td></tr> |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</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=2hhc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hhc OCA], [https://pdbe.org/2hhc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hhc RCSB], [https://www.ebi.ac.uk/pdbsum/2hhc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hhc 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=2hhc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hhc OCA], [https://pdbe.org/2hhc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hhc RCSB], [https://www.ebi.ac.uk/pdbsum/2hhc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hhc ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q9AQ17_BRASW Q9AQ17_BRASW] | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2hhc ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2hhc ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The fucosyltransferase NodZ is involved in the biosynthesis of the nodulation factor in nitrogen-fixing symbiotic bacteria. It catalyzes alpha1,6 transfer of l-fucose from GDP-fucose to the reducing residue of the synthesized Nod oligosaccharide. We present the structure of the NodZ protein from Bradyrhizobium expressed in Escherichia coli and crystallized in the presence of phosphate ions in two crystal forms. The enzyme is arranged into two domains of nearly equal size. Although NodZ falls in one broad class (GT-B) with other two-domain glycosyltransferases, the topology of its domains deviates from the canonical Rossmann fold, with particularly high distortions in the N-terminal domain. Mutational data combined with structural and sequence alignments indicate residues of potential importance in GDP-fucose binding or in the catalytic mechanism. They are all clustered in three conserved sequence motifs located in the C-terminal domain. | ||
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| - | High-resolution structure of NodZ fucosyltransferase involved in the biosynthesis of the nodulation factor.,Brzezinski K, Stepkowski T, Panjikar S, Bujacz G, Jaskolski M Acta Biochim Pol. 2007;54(3):537-49. Epub 2007 Aug 30. PMID:17762900<ref>PMID:17762900</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 2hhc" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[NodS|NodS]] | *[[NodS|NodS]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Bradyrhizobium sp. WM9]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Brzezinski | + | [[Category: Brzezinski K]] |
| - | [[Category: Bujacz | + | [[Category: Bujacz G]] |
| - | [[Category: Jaskolski | + | [[Category: Jaskolski M]] |
| - | [[Category: Panjikar | + | [[Category: Panjikar S]] |
| - | [[Category: Stepkowski | + | [[Category: Stepkowski T]] |
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Current revision
Crystal structure of fucosyltransferase NodZ from Bradyrhizobium
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