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| [[Image:3d31.jpg|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_3d31| PDB=3d31 | SCENE= }} | | {{STRUCTURE_3d31| PDB=3d31 | SCENE= }} |
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| '''ModBC from Methanosarcina acetivorans'''
| | ===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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_18511655}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 18511655 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_18511655}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Transport]] | | [[Category: Transport]] |
| [[Category: Transport protein]] | | [[Category: Transport protein]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 11 10:51:13 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 17:07:49 2008'' |