5d1i: Difference between revisions
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The | ==Structure of Cyclic nucleotide-binding-like protein from Brucella abortus bv. 1 str. 9-941== | ||
<StructureSection load='5d1i' size='340' side='right'caption='[[5d1i]], [[Resolution|resolution]] 2.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5d1i]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Brucella_abortus_bv._1_str._9-941 Brucella abortus bv. 1 str. 9-941]. 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 [https://proteopedia.org/fgij/fg.htm?mol=5D1I FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</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></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=5d1i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d1i OCA], [https://pdbe.org/5d1i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5d1i RCSB], [https://www.ebi.ac.uk/pdbsum/5d1i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5d1i ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q57AQ0_BRUAB Q57AQ0_BRUAB] | |||
<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> | |||
[[Category: | </div> | ||
[[Category: Dong | <div class="pdbe-citations 5d1i" style="background-color:#fffaf0;"></div> | ||
[[Category: Gao | == References == | ||
[[Category: | <references/> | ||
[[Category: | __TOC__ | ||
</StructureSection> | |||
[[Category: Brucella abortus bv. 1 str. 9-941]] | |||
[[Category: Large Structures]] | |||
[[Category: Dong J]] | |||
[[Category: Gao Y]] | |||
[[Category: He Z]] | |||
[[Category: Li X]] | |||