1q1e: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
Line 1: Line 1:
[[Image:1q1e.jpg|left|200px]]
[[Image:1q1e.jpg|left|200px]]


{{Structure
<!--
|PDB= 1q1e |SIZE=350|CAPTION= <scene name='initialview01'>1q1e</scene>, resolution 2.90&Aring;
The line below this paragraph, containing "STRUCTURE_1q1e", creates the "Structure Box" on the page.
|SITE=
You may change the PDB parameter (which sets the PDB file loaded into the applet)
|LIGAND=
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
|ACTIVITY=
or leave the SCENE parameter empty for the default display.
|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])
-->
|DOMAIN=
{{STRUCTURE_1q1e|  PDB=1q1e |  SCENE= }}  
|RELATEDENTRY=[[1q1b|1Q1B]], [[1q12|1Q12]]
|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>
}}


'''The ATPase component of E. coli maltose transporter (MalK) in the nucleotide-free form'''
'''The ATPase component of E. coli maltose transporter (MalK) in the nucleotide-free form'''
Line 30: Line 27:
[[Category: Lu, G.]]
[[Category: Lu, G.]]
[[Category: Quiocho, F A.]]
[[Category: Quiocho, F A.]]
[[Category: atp-binding cassette]]
[[Category: Atp-binding cassette]]
[[Category: nucleotide-free form]]
[[Category: Nucleotide-free form]]
[[Category: sugar transport]]
[[Category: Sugar transport]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 05:44:53 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:07:31 2008''

Revision as of 05:44, 3 May 2008

File:1q1e.jpg

Template:STRUCTURE 1q1e

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


OverviewOverview

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.

About this StructureAbout this Structure

1Q1E is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

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:14527411 Page seeded by OCA on Sat May 3 05:44:53 2008

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

OCA