4zir

From Proteopedia

(Difference between revisions)

Revision as of 14:21, 27 April 2017

Crystal structure of EcfAA' heterodimer bound to AMPPNP

Structural highlights

4zir is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Related:	4hlu
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[ECFA2_THEMA] ATP-binding (A) component of a common energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates (Probable). Expression of the complex plus RibU in E.coli allows riboflavin uptake; uptake does not occur in the absence of RibU or the EcfA1A2T complex.^[1] [ECFA1_THEMA] ATP-binding (A) component of a common energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates (Probable). Expression of the complex plus RibU in E.coli allows riboflavin uptake; uptake does not occur in the absence of RibU or the EcfA1A2T complex.[HAMAP-Rule:MF_01710]^[2]

Publication Abstract from PubMed

ECF transporters are a family of active transporters for vitamins. They are composed of four subunits: a membrane-embedded substrate-binding subunit (EcfS), a transmembrane coupling subunit (EcfT) and two ATP-binding-cassette ATPases (EcfA and EcfA'). We have investigated the mechanism of the ECF transporter for riboflavin from the pathogen Listeria monocytogenes, LmECF-RibU. Using structural and biochemical approaches, we found that ATP binding to the EcfAA' ATPases drives a conformational change that dissociates the S subunit from the EcfAA'T ECF module. Upon release from the ECF module, the RibU S subunit then binds the riboflavin transport substrate. We also find that S subunits for distinct substrates compete for the ATP-bound state of the ECF module. Our results explain how ECF transporters capture the transport substrate and reproduce the in vivo observations on S-subunit competition for which the family was named.

ATP binding drives substrate capture in an ECF transporter by a release-and-catch mechanism.,Karpowich NK, Song JM, Cocco N, Wang DN Nat Struct Mol Biol. 2015 Jun 8. doi: 10.1038/nsmb.3040. PMID:26052893^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Karpowich NK, Wang DN. Assembly and mechanism of a group II ECF transporter. Proc Natl Acad Sci U S A. 2013 Feb 12;110(7):2534-9. doi:, 10.1073/pnas.1217361110. Epub 2013 Jan 28. PMID:23359690 doi:http://dx.doi.org/10.1073/pnas.1217361110
↑ Karpowich NK, Wang DN. Assembly and mechanism of a group II ECF transporter. Proc Natl Acad Sci U S A. 2013 Feb 12;110(7):2534-9. doi:, 10.1073/pnas.1217361110. Epub 2013 Jan 28. PMID:23359690 doi:http://dx.doi.org/10.1073/pnas.1217361110
↑ Karpowich NK, Song JM, Cocco N, Wang DN. ATP binding drives substrate capture in an ECF transporter by a release-and-catch mechanism. Nat Struct Mol Biol. 2015 Jun 8. doi: 10.1038/nsmb.3040. PMID:26052893 doi:http://dx.doi.org/10.1038/nsmb.3040

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4zir"

@@ Line 1: / Line 1: @@
 ==Crystal structure of EcfAA' heterodimer bound to AMPPNP==
 <StructureSection load='4zir' size='340' side='right' caption='[[4zir]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4hlu|4hlu]]</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=4zir FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zir OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4zir RCSB], [http://www.ebi.ac.uk/pdbsum/4zir 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=4zir FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zir OCA], [http://pdbe.org/4zir PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4zir RCSB], [http://www.ebi.ac.uk/pdbsum/4zir PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4zir ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 17: / Line 18: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4zir" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

4zir

From Proteopedia

Revision as of 14:21, 27 April 2017

Crystal structure of EcfAA' heterodimer bound to AMPPNP

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox