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3fh6

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Revision as of 06:42, 1 November 2017

Crystal structure of the resting state maltose transporter from E. coli

Structural highlights

3fh6 is a 8 chain structure with sequence from Ecoli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	2r6g, 1q1b, 1q1e
Gene:	b4033, JW3993, malF (ECOLI), b4032, JW3992, malG (ECOLI), b4035, JW3995, malK (ECOLI)
Activity:	Maltose-transporting ATPase, with EC number 3.6.3.19
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[MALF_ECOLI] Part of the binding-protein-dependent transport system for maltose; probably responsible for the translocation of the substrate across the membrane. [MALK_ECOLI] Part of the ABC transporter complex MalEFGK involved in maltose/maltodextrin import. Responsible for energy coupling to the transport system. [MALG_ECOLI] Part of the binding-protein-dependent transport system for maltose; probably responsible for the translocation of the substrate across the membrane.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

ATP-binding cassette transporters couple ATP hydrolysis to substrate translocation through an alternating access mechanism, but the nature of the conformational changes in a transport cycle remains elusive. Previously we reported the structure of the maltose transporter MalFGK(2) in an outward-facing conformation in which the transmembrane (TM) helices outline a substrate-binding pocket open toward the periplasmic surface and ATP is poised for hydrolysis along the closed nucleotide-binding dimer interface. Here we report the structure of the nucleotide-free maltose transporter in which the substrate binding pocket is only accessible from the cytoplasm and the nucleotide-binding interface is open. Comparison of the same transporter crystallized in two different conformations reveals that alternating access involves rigid-body rotations of the TM subdomains that are coupled to the closure and opening of the nucleotide-binding domain interface. The comparison also reveals that point mutations enabling binding protein-independent transport line dynamic interfaces in the TM region.

Alternating access in maltose transporter mediated by rigid-body rotations.,Khare D, Oldham ML, Orelle C, Davidson AL, Chen J Mol Cell. 2009 Feb 27;33(4):528-36. PMID:19250913^[1]

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

References

↑ Khare D, Oldham ML, Orelle C, Davidson AL, Chen J. Alternating access in maltose transporter mediated by rigid-body rotations. Mol Cell. 2009 Feb 27;33(4):528-36. PMID:19250913 doi:S1097-2765(09)00100-2

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3fh6"

@@ Line 1: / Line 1: @@
 ==Crystal structure of the resting state maltose transporter from E. coli==
 <StructureSection load='3fh6' size='340' side='right' caption='[[3fh6]], [[Resolution|resolution]] 4.50&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b4033, JW3993, malF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI]), b4032, JW3992, malG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI]), b4035, JW3995, malK ([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/Maltose-transporting_ATPase Maltose-transporting ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.19 3.6.3.19] </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=3fh6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fh6 OCA], [http://pdbe.org/3fh6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3fh6 RCSB], [http://www.ebi.ac.uk/pdbsum/3fh6 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=3fh6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fh6 OCA], [http://pdbe.org/3fh6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3fh6 RCSB], [http://www.ebi.ac.uk/pdbsum/3fh6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3fh6 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 29: / Line 30: @@
 </div>
 <div class="pdbe-citations 3fh6" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Maltose-binding protein|Maltose-binding protein]]
 == References ==
 <references/>

3fh6

From Proteopedia

Revision as of 06:42, 1 November 2017

Crystal structure of the resting state maltose transporter from E. coli

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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