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1f3o

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[[Image:1f3o.gif|left|200px]]
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{{STRUCTURE_1f3o| PDB=1f3o | SCENE= }}
{{STRUCTURE_1f3o| PDB=1f3o | SCENE= }}
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'''Crystal structure of MJ0796 ATP-binding cassette'''
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===Crystal structure of MJ0796 ATP-binding cassette===
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==Overview==
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The crystal structure of the MJ0796 ATP-binding cassette, a member of the o228/LolD transporter family, has been determined at 2.7-A resolution with MgADP bound at its active site. Comparing this structure with that of the ATP-bound form of the HisP ATP-binding cassette (Hung, L. W., Wang, I. X., Nikaido, K., Liu, P. Q., Ames, G. F., and Kim, S. H. (1998) Nature 396, 703-707) shows a 5-A withdrawal of a phylogenetically invariant glutamine residue from contact with the gamma-phosphate of ATP in the active site. This glutamine is located in a protein segment that links the rigid F(1)-type ATP-binding core of the enzyme to an ABC transporter-specific alpha-helical subdomain that moves substantially away from the active site in the MgADP-bound structure of MJ0796 compared with the ATP-bound structure of HisP. A similar conformational effect is observed in the MgADP-bound structure of MJ1267 (Karpowich, N., et al. (2001) Structure, in press), establishing the withdrawal of the glutamine and the coupled outward rotation of the alpha-helical subdomain as consistent consequences of gamma-phosphate release from the active site of the transporter. Considering this subdomain movement in the context of a leading model for the physiological dimer of cassettes present in ABC transporters indicates that it produces a modest mechanical change that is likely to play a role in facilitating nucleotide exchange out of the ATPase active site. Finally, it is noteworthy that one of the intersubunit packing interactions in the MJ0796 crystal involves antiparallel beta-type hydrogen bonding interactions between the outermost beta-strands in the two core beta-sheets, leading to their fusion into a single extended beta-sheet, a type of structural interaction that has been proposed to play a role in mediating the aggregation of beta-sheet-containing proteins.
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(as it appears on PubMed at http://www.pubmed.gov), where 11402022 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11402022}}
==About this Structure==
==About this Structure==
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[[Category: Yuan, Y R.]]
[[Category: Yuan, Y R.]]
[[Category: Transporter]]
[[Category: Transporter]]
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Revision as of 23:37, 30 June 2008

Image:1f3o.png

Template:STRUCTURE 1f3o

Crystal structure of MJ0796 ATP-binding cassette

Template:ABSTRACT PUBMED 11402022

About this Structure

1F3O is a Single protein structure of sequence from Methanocaldococcus jannaschii. Full crystallographic information is available from OCA.

Reference

The crystal structure of the MJ0796 ATP-binding cassette. Implications for the structural consequences of ATP hydrolysis in the active site of an ABC transporter., Yuan YR, Blecker S, Martsinkevich O, Millen L, Thomas PJ, Hunt JF, J Biol Chem. 2001 Aug 24;276(34):32313-21. Epub 2001 Jun 11. PMID:11402022

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