3t56

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (10:02, 1 March 2024) (edit) (undo)
 
(3 intermediate revisions not shown.)
Line 1: Line 1:
 +
==Crystal structure of the pre-extrusion state of the CusBA adaptor-transporter complex==
==Crystal structure of the pre-extrusion state of the CusBA adaptor-transporter complex==
-
<StructureSection load='3t56' size='340' side='right' caption='[[3t56]], [[Resolution|resolution]] 3.42&Aring;' scene=''>
+
<StructureSection load='3t56' size='340' side='right'caption='[[3t56]], [[Resolution|resolution]] 3.42&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[3t56]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3T56 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3T56 FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[3t56]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3T56 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3T56 FirstGlance]. <br>
-
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene><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]] 3.42&#8491;</td></tr>
-
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3t51|3t51]], [[3t53|3t53]]</td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene></td></tr>
-
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b0575, cusA, CusB, JW0564, ybdE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]), cusB, ylcD, b0574, JW0563 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</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=3t56 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t56 OCA], [https://pdbe.org/3t56 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3t56 RCSB], [https://www.ebi.ac.uk/pdbsum/3t56 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3t56 ProSAT]</span></td></tr>
-
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3t56 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t56 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3t56 RCSB], [http://www.ebi.ac.uk/pdbsum/3t56 PDBsum]</span></td></tr>
+
</table>
-
<table>
+
== Function ==
-
<div style="background-color:#fffaf0;">
+
[https://www.uniprot.org/uniprot/CUSA_ECOLI CUSA_ECOLI] Part of a cation efflux system that mediates resistance to copper and silver.<ref>PMID:11399769</ref> <ref>PMID:12813074</ref>
-
== Publication Abstract from PubMed ==
+
-
Gram-negative bacteria expel various toxic chemicals via tripartite efflux pumps belonging to the resistance-nodulation-cell division superfamily. These pumps span both the inner and outer membranes of the cell. The three components of these tripartite systems are an inner-membrane, substrate-binding transporter (or pump); a periplasmic membrane fusion protein (or adaptor); and an outer-membrane-anchored channel. These three efflux proteins interact in the periplasmic space to form the three-part complexes. We previously presented the crystal structures of both the inner-membrane transporter CusA and membrane fusion protein CusB of the CusCBA tripartite efflux system from Escherichia coli. We also described the co-crystal structure of the CusBA adaptor-transporter, revealing that the trimeric CusA efflux pump assembles with six CusB protein molecules to form the complex CusB(6)-CusA(3). We here report three different conformers of the crystal structures of CusBA-Cu(I), suggesting a mechanism on how Cu(I) binding initiates a sequence of conformational transitions in the transport cycle. Genetic analysis and transport assays indicate that charged residues, in addition to the methionine pairs and clusters, are essential for extruding metal ions out of the cell.
+
-
 
+
-
Charged Amino Acids (R83, E567, D617, E625, R669, and K678) of CusA Are Required for Metal Ion Transport in the Cus Efflux System.,Su CC, Long F, Lei HT, Bolla JR, Do SV, Rajashankar KR, Yu EW J Mol Biol. 2012 Jun 6. PMID:22683351<ref>PMID:22683351</ref>
+
-
 
+
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Escherichia coli]]
+
[[Category: Escherichia coli K-12]]
-
[[Category: Long, F.]]
+
[[Category: Large Structures]]
-
[[Category: Su, C C.]]
+
[[Category: Long F]]
-
[[Category: Yu, E W.]]
+
[[Category: Su C-C]]
-
[[Category: Transmembrane helix]]
+
[[Category: Yu EW]]
-
[[Category: Transport protein]]
+

Current revision

Crystal structure of the pre-extrusion state of the CusBA adaptor-transporter complex

PDB ID 3t56

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3t56"
Personal tools