3fh6: Difference between revisions

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{{Seed}}
[[Image:3fh6.png|left|200px]]


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==Crystal structure of the resting state maltose transporter from E. coli==
The line below this paragraph, containing "STRUCTURE_3fh6", creates the "Structure Box" on the page.
<StructureSection load='3fh6' size='340' side='right'caption='[[3fh6]], [[Resolution|resolution]] 4.50&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[3fh6]] is a 8 chain structure with sequence from [https://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=3FH6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FH6 FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 4.5&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3fh6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fh6 OCA], [https://pdbe.org/3fh6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fh6 RCSB], [https://www.ebi.ac.uk/pdbsum/3fh6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fh6 ProSAT]</span></td></tr>
{{STRUCTURE_3fh6|  PDB=3fh6  |  SCENE=  }}
</table>
== Function ==
[https://www.uniprot.org/uniprot/MALF_ECOLI MALF_ECOLI] Part of the binding-protein-dependent transport system for maltose; probably responsible for the translocation of the substrate across the membrane.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fh/3fh6_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3fh6 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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.


===Crystal structure of the resting state maltose transporter from E. coli===
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<ref>PMID:19250913</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3fh6" style="background-color:#fffaf0;"></div>


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==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_19250913}}, adds the Publication Abstract to the page
*[[Maltose-binding protein 3D structures|Maltose-binding protein 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 19250913 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_19250913}}
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Escherichia coli K-12]]
3FH6 is a [[Protein complex]] structure of sequences 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=3FH6 OCA].
[[Category: Large Structures]]
 
[[Category: Chen J]]
==Reference==
[[Category: Davidson AL]]
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:[http://www.ncbi.nlm.nih.gov/pubmed/19250913 19250913]
[[Category: Khare D]]
[[Category: Escherichia coli k-12]]
[[Category: Oldham ML]]
[[Category: Maltose-transporting ATPase]]
[[Category: Orelle C]]
[[Category: Protein complex]]
[[Category: Pdbx_ordinal=, <PDBx:audit_author.]]
[[Category: Abc transporter]]
[[Category: Atp-binding]]
[[Category: Cell inner membrane]]
[[Category: Cell membrane]]
[[Category: Ground state]]
[[Category: Hydrolase]]
[[Category: Maltose transporter]]
[[Category: Membrane]]
[[Category: Membrane protein]]
[[Category: Nucleotide-binding]]
[[Category: Sugar transport]]
[[Category: Transmembrane]]
[[Category: Transport]]
[[Category: Transport protein]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Mar 25 20:28:05 2009''

Latest revision as of 09:46, 6 September 2023

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

Structural highlights

3fh6 is a 8 chain structure with sequence from Escherichia coli K-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 4.5Å
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.

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.

See Also

References

  1. ↑ 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

3fh6, resolution 4.50Å

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