1q1e: Difference between revisions

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[[Image:1q1e.jpg|left|200px]]


{{Structure
==The ATPase component of E. coli maltose transporter (MalK) in the nucleotide-free form==
|PDB= 1q1e |SIZE=350|CAPTION= <scene name='initialview01'>1q1e</scene>, resolution 2.90&Aring;
<StructureSection load='1q1e' size='340' side='right'caption='[[1q1e]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND=  
<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>
|ACTIVITY=  
</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>
|GENE= MALK OR B4035 OR Z5633 OR ECS5018 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
<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>
|DOMAIN=
</table>
|RELATEDENTRY=[[1q1b|1Q1B]], [[1q12|1Q12]]
== Function ==
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1q1e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q1e OCA], [http://www.ebi.ac.uk/pdbsum/1q1e PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1q1e RCSB]</span>
[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.
}}
== Evolutionary Conservation ==
 
[[Image:Consurf_key_small.gif|200px|right]]
'''The ATPase component of E. coli maltose transporter (MalK) in the nucleotide-free form'''
Check<jmol>
 
  <jmolCheckbox>
 
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/q1/1q1e_consurf.spt"</scriptWhenChecked>
==Overview==
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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.
    <text>to colour the structure by Evolutionary Conservation</text>
 
  </jmolCheckbox>
==About this Structure==
</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].
1Q1E is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q1E OCA].  
<div style="clear:both"></div>
 
__TOC__
==Reference==
</StructureSection>
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://www.ncbi.nlm.nih.gov/pubmed/14527411 14527411]
[[Category: Escherichia coli K-12]]
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Chen J]]
[[Category: Chen, J.]]
[[Category: Davidson AL]]
[[Category: Davidson, A L.]]
[[Category: Lin J]]
[[Category: Lin, J.]]
[[Category: Lu G]]
[[Category: Lu, G.]]
[[Category: Quiocho FA]]
[[Category: Quiocho, F A.]]
[[Category: atp-binding cassette]]
[[Category: nucleotide-free form]]
[[Category: sugar transport]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:07:31 2008''

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

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