1g29

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[[Image:1g29.jpg|left|200px]]
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{{STRUCTURE_1g29| PDB=1g29 | SCENE= }}
{{STRUCTURE_1g29| PDB=1g29 | SCENE= }}
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'''MALK'''
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===MALK===
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==Overview==
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The members of the ABC transporter family transport a wide variety of molecules into or out of cells and cellular compartments. Apart from a translocation pore, each member possesses two similar nucleoside triphosphate-binding subunits or domains in order to couple the energy-providing reaction with transport. In the maltose transporter of several Gram-negative bacteria and the archaeon Thermo coccus litoralis, the nucleoside triphosphate-binding subunit contains a C-terminal regulatory domain. A dimer of the subunit is attached cytoplasmically to the translocation pore. Here we report the crystal structure of this dimer showing two bound pyrophosphate molecules at 1.9 A resolution. The dimer forms by association of the ATPase domains, with the two regulatory domains attached at opposite poles. Significant deviation from 2-fold symmetry is seen at the interface of the dimer and in the regions corresponding to those residues known to be in contact with the translocation pore. The structure and its relationship to function are discussed in the light of known mutations from the homologous Escherichia coli and Salmonella typhimurium proteins.
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The line below this paragraph, {{ABSTRACT_PUBMED_11080142}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 11080142 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11080142}}
==About this Structure==
==About this Structure==
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[[Category: Atpase]]
[[Category: Atpase]]
[[Category: Maltose uptake and regulation]]
[[Category: Maltose uptake and regulation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:02:42 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 04:17:57 2008''

Revision as of 01:17, 1 July 2008

Image:1g29.png

Template:STRUCTURE 1g29

MALK

Template:ABSTRACT PUBMED 11080142

About this Structure

1G29 is a Single protein structure of sequence from Thermococcus litoralis. Full crystallographic information is available from OCA.

Reference

Crystal structure of MalK, the ATPase subunit of the trehalose/maltose ABC transporter of the archaeon Thermococcus litoralis., Diederichs K, Diez J, Greller G, Muller C, Breed J, Schnell C, Vonrhein C, Boos W, Welte W, EMBO J. 2000 Nov 15;19(22):5951-61. PMID:11080142

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