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| [[Image:1q1e.jpg|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1q1e| PDB=1q1e | SCENE= }} | | {{STRUCTURE_1q1e| PDB=1q1e | SCENE= }} |
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| '''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=== |
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| ==Overview==
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| 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. | | The line below this paragraph, {{ABSTRACT_PUBMED_14527411}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 14527411 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_14527411}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[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 Mon Jul 28 17:45:15 2008'' |