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4huq

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Revision as of 07:04, 25 December 2014

Crystal Structure of a transporter

Structural highlights

4huq is a 4 chain structure with sequence from Lactobacillus brevis atcc 367. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	cbiO1, ecfA1, LVIS_1661, unknown transporter (Lactobacillus brevis ATCC 367), ecfA2, cbiO2, LVIS_1662 (Lactobacillus brevis ATCC 367), LVIS_0823 (Lactobacillus brevis ATCC 367), ecfT, LVIS_1660 (Lactobacillus brevis ATCC 367)
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[ECFT_LACBA] Transmembrane (T) component of an 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 (By similarity). [ECFA1_LACBA] Part 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 (By similarity). [ECFA2_LACBA] Part 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 (By similarity).

Publication Abstract from PubMed

ATP-binding cassette (ABC) transporters, composed of importers and exporters, form one of the biggest protein superfamilies that transport a variety of substrates across the membrane, powered by ATP hydrolysis. Most ABC transporters are composed of two transmembrane domains and two cytoplasmic nucleotide-binding domains. Also, importers from prokaryotes usually have extra solute-binding proteins in the periplasm that are responsible for the binding of substrates. Structures of importers have been reported that suggested a two-state model for the transport mechanism. Energy-coupling factor (ECF) transporters belong to a new class of ATP-binding cassette importers. Each ECF transporter comprises an energy-coupling module consisting of a transmembrane T protein (EcfT), two nucleotide-binding proteins (EcfA and EcfA'), and another transmembrane substrate-specific binding S protein (EcfS). Despite the similarities with ABC transporters, ECF transporters have different organizational and functional properties. The lack of solute-binding proteins in ECF transporters differentiates them clearly from the canonical ABC importers. Previously reported structures of the EcfS proteins RibU and ThiT clearly demonstrated the binding site of substrate riboflavin and thiamine, respectively. However, the organization of the four different components and the transport mechanism of ECF transporters remain unknown. Here we present the structure of an intact folate ECF transporter from Lactobacillus brevis at a resolution of 3 A. This structure was captured in an inward-facing, nucleotide-free conformation with no bound substrate. The folate-binding protein FolT is nearly parallel to the membrane and is bound almost entirely by EcfT, which adopts an L shape and connects to EcfA and EcfA' through two coupling helices. Two conserved XRX motifs from the coupling helices of EcfT have a vital role in energy coupling by docking into EcfA-EcfA'. We propose a transport model that involves a substantial conformational change of FolT.

Crystal structure of a folate energy-coupling factor transporter from Lactobacillus brevis.,Xu K, Zhang M, Zhao Q, Yu F, Guo H, Wang C, He F, Ding J, Zhang P Nature. 2013 Apr 14. doi: 10.1038/nature12046. PMID:23584589^[1]

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

References

↑ Xu K, Zhang M, Zhao Q, Yu F, Guo H, Wang C, He F, Ding J, Zhang P. Crystal structure of a folate energy-coupling factor transporter from Lactobacillus brevis. Nature. 2013 Apr 14. doi: 10.1038/nature12046. PMID:23584589 doi:10.1038/nature12046

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/4huq"

@@ Line 6: / Line 6: @@
 <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=4huq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4huq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4huq RCSB], [http://www.ebi.ac.uk/pdbsum/4huq PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/ECFT_LACBA ECFT_LACBA]] Transmembrane (T) component of an 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 (By similarity). [[http://www.uniprot.org/uniprot/ECFA1_LACBA ECFA1_LACBA]] Part 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 (By similarity). [[http://www.uniprot.org/uniprot/ECFA2_LACBA ECFA2_LACBA]] Part 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 (By similarity).
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

4huq

From Proteopedia

Revision as of 07:04, 25 December 2014

Crystal Structure of a transporter

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

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