5d1i
From Proteopedia
(Difference between revisions)
Line 4: | Line 4: | ||
<table><tr><td colspan='2'>[[5d1i]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5D1I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5D1I FirstGlance]. <br> | <table><tr><td colspan='2'>[[5d1i]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5D1I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5D1I FirstGlance]. <br> | ||
</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> | </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='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=5d1i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d1i OCA], [http://www.rcsb.org/pdb/explore.do?structureId=5d1i RCSB], [http://www.ebi.ac.uk/pdbsum/5d1i PDBsum]</span></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=5d1i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d1i OCA], [http://pdbe.org/5d1i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5d1i RCSB], [http://www.ebi.ac.uk/pdbsum/5d1i PDBsum]</span></td></tr> |
</table> | </table> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | The cyclic nucleotide-binding (CNB)-like protein (CNB-L) from Brucella abortus shares sequence homology with CNB domain-containing proteins. We determined the crystal structure of CNB-L at 2.0 A resolution in the absence of its C-terminal helix and nucleotide. The 3D structure of CNB-L is in a two-fold symmetric form. Each protomer shows high structure similarity to that of cGMP-binding domain-containing proteins, and likely mimics their nucleotide-free conformation. A key residue, Glu17, mediates the dimerization and prevents binding of cNMP to the canonical ligand-pocket. The structurally observed dimer of CNB-L is stable in solution, and thus is likely to be biologically relevant. | ||
+ | |||
+ | Crystal structure of cyclic nucleotide-binding-like protein from Brucella abortus.,He Z, Gao Y, Dong J, Ke Y, Li X, Chen Z, Zhang XC Biochem Biophys Res Commun. 2015 Dec 25;468(4):647-52. doi:, 10.1016/j.bbrc.2015.11.005. Epub 2015 Nov 6. PMID:26549229<ref>PMID:26549229</ref> | ||
+ | |||
+ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
+ | <div class="pdbe-citations 5d1i" style="background-color:#fffaf0;"></div> | ||
+ | == References == | ||
+ | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> |
Revision as of 12:11, 13 January 2016
Structure of Cyclic nucleotide-binding-like protein from Brucella abortus bv. 1 str. 9-941
|
Categories: Dong, J | Gao, Y | He, Z | Li, X | Beta barrel | Unknown function