4fi3

From Proteopedia

(Difference between revisions)

Revision as of 05:59, 5 August 2016

Structure of vitamin B12 transporter BtuCD-F in a nucleotide-bound state

Structural highlights

4fi3 is a 5 chain structure with sequence from Ecoli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Gene:	btuC, b1711, JW1701 (ECOLI), btuD, b1709, JW1699 (ECOLI), btuF, yadT, b0158, JW0154 (ECOLI)
Activity:	Vitamin B12-transporting ATPase, with EC number 3.6.3.33
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[BTUC_ECOLI] Part of the ABC transporter complex BtuCDF involved in vitamin B12 import. Involved in the translocation of the substrate across the membrane.[HAMAP-Rule:MF_01004] [BTUF_ECOLI] Part of the ABC transporter complex BtuCDF involved in vitamin B12 import. Binds vitamin B12 and delivers it to the periplasmic surface of BtuC.^[1] [BTUD_ECOLI] Part of the ABC transporter complex BtuCDF involved in vitamin B12 import. Responsible for energy coupling to the transport system (By similarity).

Publication Abstract from PubMed

The ATP-binding cassette (ABC) transporter BtuCD mediates the uptake of vitamin B(12) across the inner membrane of Escherichia coli. Previous structures have shown the conformations of apo states, but the transport mechanism has remained unclear. Here we report the 3.5 A crystal structure of the transporter-binding protein complex BtuCD-BtuF (BtuCD-F) trapped in an beta-gamma-imidoadenosine 5'-phosphate (AMP-PNP)-bound intermediate state. Although the ABC domains (BtuD subunits) form the expected closed sandwich dimer, the membrane-spanning BtuC subunits adopt a new conformation, with the central translocation pathway sealed by a previously unrecognized cytoplasmic gate. A fully enclosed cavity is thus formed approximately halfway across the membrane. It is large enough to accommodate a vitamin B(12) molecule, and radioligand trapping showed that liposome-reconstituted BtuCD-F indeed contains bound B(12) in the presence of AMP-PNP. In combination with engineered disulphide crosslinking and functional assays, our data suggest an unexpected peristaltic transport mechanism that is distinct from those observed in other ABC transporters.

Structure of AMP-PNP-bound vitamin B12 transporter BtuCD-F.,Korkhov VM, Mireku SA, Locher KP Nature. 2012 Oct 18;490(7420):367-72. doi: 10.1038/nature11442. Epub 2012 Sep 23. PMID:23000901^[2]

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

References

↑ Cadieux N, Bradbeer C, Reeger-Schneider E, Koster W, Mohanty AK, Wiener MC, Kadner RJ. Identification of the periplasmic cobalamin-binding protein BtuF of Escherichia coli. J Bacteriol. 2002 Feb;184(3):706-17. PMID:11790740
↑ Korkhov VM, Mireku SA, Locher KP. Structure of AMP-PNP-bound vitamin B12 transporter BtuCD-F. Nature. 2012 Oct 18;490(7420):367-72. doi: 10.1038/nature11442. Epub 2012 Sep 23. PMID:23000901 doi:http://dx.doi.org/10.1038/nature11442

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/4fi3"

@@ Line 1: / Line 1: @@
 ==Structure of vitamin B12 transporter BtuCD-F in a nucleotide-bound state==
 <StructureSection load='4fi3' size='340' side='right' caption='[[4fi3]], [[Resolution|resolution]] 3.47&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4fi3]] is a 5 chain structure with sequence from [http://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=4FI3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FI3 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4fi3]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FI3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FI3 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=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">btuC, b1711, JW1701 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 Escherichia coli K-12]), btuD, b1709, JW1699 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 Escherichia coli K-12]), btuF, yadT, b0158, JW0154 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 Escherichia coli K-12])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">btuC, b1711, JW1701 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI]), btuD, b1709, JW1699 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI]), btuF, yadT, b0158, JW0154 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Vitamin_B12-transporting_ATPase Vitamin B12-transporting ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.33 3.6.3.33] </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=4fi3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fi3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4fi3 RCSB], [http://www.ebi.ac.uk/pdbsum/4fi3 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=4fi3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fi3 OCA], [http://pdbe.org/4fi3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4fi3 RCSB], [http://www.ebi.ac.uk/pdbsum/4fi3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4fi3 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 18: / Line 19: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4fi3" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Escherichia coli k-12]]
+[[Category: Ecoli]]
 [[Category: Vitamin B12-transporting ATPase]]
 [[Category: Korkhov, V M]]

4fi3

From Proteopedia

Revision as of 05:59, 5 August 2016

Structure of vitamin B12 transporter BtuCD-F in a nucleotide-bound state

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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