1q1e: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
New page: left|200px<br /><applet load="1q1e" size="450" color="white" frame="true" align="right" spinBox="true" caption="1q1e, resolution 2.90Å" /> '''The ATPase component...
 
No edit summary
 
(14 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1q1e.jpg|left|200px]]<br /><applet load="1q1e" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1q1e, resolution 2.90&Aring;" />
'''The ATPase component of E. coli maltose transporter (MalK) in the nucleotide-free form'''<br />


==Overview==
==The ATPase component of E. coli maltose transporter (MalK) in the nucleotide-free form==
The ATPase components of ATP binding cassette (ABC) transporters power the, transporters by binding and hydrolyzing ATP. Major conformational changes, of an ATPase are revealed by crystal structures of MalK, the ATPase, subunit of the maltose transporter from Escherichia coli, in three, different dimeric configurations. While other nucleotide binding domains, or subunits display low affinity for each other in the absence of the, transmembrane segments, the MalK dimer is stabilized through interactions, of the additional C-terminal domains. In the two nucleotide-free, structures, the N-terminal nucleotide binding domains are separated to, differing degrees, and the dimer is maintained through contacts of the, C-terminal regulatory domains. In the ATP-bound form, the nucleotide, binding domains make contact and two ATPs lie buried along the dimer, interface. The two nucleotide binding domains of the dimer open and close, like a pair of tweezers, suggesting a regulatory mechanism for ATPase, activity that may be tightly coupled to translocation.
<StructureSection load='1q1e' size='340' side='right'caption='[[1q1e]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[1q1e]] is a 2 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=1Q1E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Q1E FirstGlance]. <br>
1Q1E is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1Q1E OCA].  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9&#8491;</td></tr>
 
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1q1e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q1e OCA], [https://pdbe.org/1q1e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1q1e RCSB], [https://www.ebi.ac.uk/pdbsum/1q1e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1q1e ProSAT]</span></td></tr>
==Reference==
</table>
A tweezers-like motion of the ATP-binding cassette dimer in an ABC transport cycle., Chen J, Lu G, Lin J, Davidson AL, Quiocho FA, Mol Cell. 2003 Sep;12(3):651-61. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14527411 14527411]
== Function ==
[[Category: Escherichia coli]]
[https://www.uniprot.org/uniprot/MALK_ECOLI MALK_ECOLI] Part of the ABC transporter complex MalEFGK involved in maltose/maltodextrin import. Responsible for energy coupling to the transport system.
[[Category: Single protein]]
== Evolutionary Conservation ==
[[Category: Chen, J.]]
[[Image:Consurf_key_small.gif|200px|right]]
[[Category: Davidson, A.L.]]
Check<jmol>
[[Category: Lin, J.]]
  <jmolCheckbox>
[[Category: Lu, G.]]
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/q1/1q1e_consurf.spt"</scriptWhenChecked>
[[Category: Quiocho, F.A.]]
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
[[Category: atp-binding cassette]]
    <text>to colour the structure by Evolutionary Conservation</text>
[[Category: nucleotide-free form]]
  </jmolCheckbox>
[[Category: sugar transport]]
</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=1q1e ConSurf].
 
<div style="clear:both"></div>
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:18:09 2007''
__TOC__
</StructureSection>
[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Chen J]]
[[Category: Davidson AL]]
[[Category: Lin J]]
[[Category: Lu G]]
[[Category: Quiocho FA]]

Latest revision as of 11:12, 14 February 2024

The ATPase component of E. coli maltose transporter (MalK) in the nucleotide-free formThe ATPase component of E. coli maltose transporter (MalK) in the nucleotide-free form

Structural highlights

1q1e is a 2 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 2.9Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MALK_ECOLI Part of the ABC transporter complex MalEFGK involved in maltose/maltodextrin import. Responsible for energy coupling to the transport system.

Evolutionary Conservation

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

1q1e, resolution 2.90Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=1q1e&oldid=4053582"