1q12: Difference between revisions

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{{Seed}}
[[Image:1q12.png|left|200px]]
[[Image:1q12.png|left|200px]]


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{{STRUCTURE_1q12|  PDB=1q12  |  SCENE=  }}  
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===Crystal Structure of the ATP-bound E. coli MalK===
===Crystal Structure of the ATP-bound E. coli MalK===


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{{ABSTRACT_PUBMED_14527411}}
{{ABSTRACT_PUBMED_14527411}}


==About this Structure==
==About this Structure==
1Q12 is a 4 chains structure of sequences 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=1Q12 OCA].  
[[1q12]] is a 4 chain structure with 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=1Q12 OCA].  


==Reference==
==Reference==
<ref group="xtra">PMID:14527411</ref><references group="xtra"/>
<ref group="xtra">PMID:014527411</ref><ref group="xtra">PMID:018033289</ref><references group="xtra"/>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Chen, J.]]
[[Category: Chen, J.]]
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[[Category: Quiocho, F A.]]
[[Category: Quiocho, F A.]]
[[Category: Atp-binding cassette]]
[[Category: Atp-binding cassette]]
 
[[Category: Transport protein]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 04:40:26 2009''

Revision as of 09:52, 2 January 2013

File:1q12.png

Template:STRUCTURE 1q12

Crystal Structure of the ATP-bound E. coli MalK

Template:ABSTRACT PUBMED 14527411

About this Structure

1q12 is a 4 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

  1. Chen J, Lu G, Lin J, Davidson AL, Quiocho FA. A tweezers-like motion of the ATP-binding cassette dimer in an ABC transport cycle. Mol Cell. 2003 Sep;12(3):651-61. PMID:14527411
  2. Oldham ML, Khare D, Quiocho FA, Davidson AL, Chen J. Crystal structure of a catalytic intermediate of the maltose transporter. Nature. 2007 Nov 22;450(7169):515-21. PMID:18033289 doi:10.1038/nature06264

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