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4zir

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Revision as of 06:56, 19 June 2019

Crystal structure of EcfAA' heterodimer bound to AMPPNP

Structural highlights

4zir is a 2 chain structure with sequence from Thema. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Related:	4hlu
Gene:	ecfA2, ecfA, ecfA', TM_0222 (THEMA), ecfA1, cbiO, ecfA', TM_1663 (THEMA)
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=''>
+<StructureSection load='4zir' size='340' side='right'caption='[[4zir]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4zir]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZIR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ZIR FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4zir]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Thema Thema]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZIR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ZIR FirstGlance]. <br>
 </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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ecfA2, ecfA, ecfA', TM_0222 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243274 THEMA]), ecfA1, cbiO, ecfA', TM_1663 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243274 THEMA])</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>
@@ Line 23: / Line 24: @@
 __TOC__
 </StructureSection>
+[[Category: Large Structures]]
+[[Category: Thema]]
 [[Category: Cocco, N]]
 [[Category: Karpowich, N K]]

4zir

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Revision as of 06:56, 19 June 2019

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

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