3d31

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{{Seed}}
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{{STRUCTURE_3d31| PDB=3d31 | SCENE= }}
{{STRUCTURE_3d31| PDB=3d31 | SCENE= }}
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'''ModBC from Methanosarcina acetivorans'''
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===ModBC from Methanosarcina acetivorans===
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==Overview==
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Transport across cellular membranes is an essential process that is catalyzed by diverse membrane transport proteins. The turnover rates of certain transporters are inhibited by their substrates in a process termed trans-inhibition, whose structural basis is poorly understood. Here we present the crystal structure of a molybdate/tungstate ABC transporter (ModBC) from Methanosarcina acetivorans in a trans-inhibited state. The regulatory domains of the nucleotide-binding subunits are in close contact and provide two oxyanion binding pockets at the shared interface. By specifically binding to these pockets, molybdate or tungstate prevent ATPase activity and lock the transporter in an inward-facing conformation, with the catalytic motifs of the nucleotide-binding domains separated. This allosteric effect prevents the transporter from switching between the inward-facing and the outward-facing states, thus interfering with the alternating access and release mechanism.
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(as it appears on PubMed at http://www.pubmed.gov), where 18511655 is the PubMed ID number.
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{{ABSTRACT_PUBMED_18511655}}
==About this Structure==
==About this Structure==
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[[Category: Transport]]
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Revision as of 14:07, 28 July 2008

Image:3d31.png

Template:STRUCTURE 3d31

ModBC from Methanosarcina acetivorans

Template:ABSTRACT PUBMED 18511655

About this Structure

3D31 is a Protein complex structure of sequences from Methanosarcina acetivorans. Full crystallographic information is available from OCA.

Reference

Structural Basis of Trans-Inhibition in a Molybdate/tungstate ABC Transporter., Gerber S, Comellas-Bigler M, Goetz BA, Locher KP, Science. 2008 May 29;. PMID:18511655

Page seeded by OCA on Mon Jul 28 17:07:49 2008

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