1gml: Difference between revisions
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==Overview== | ==Overview== | ||
The chaperonin containing TCP-1 (CCT, also known as TRiC) is the only, member of the chaperonin family found in the cytosol of eukaryotes. Like, other chaperonins, it assists the folding of newly synthesised proteins., It is, however, unique in its specificity towards only a small subset of, non-native proteins. We determined two crystal structures of mouse, CCTgamma apical domain at 2.2 A and 2.8 A resolution. They reveal a, surface patch facing the inside of the torus that is highly evolutionarily, conserved and specific for the CCTgamma apical domain. This putative, substrate-binding region consists of predominantly positively charged, side-chains. It suggests that the specificity of this apical domain, towards its substrate, partially folded tubulin, is conferred by polar and, .. | The chaperonin containing TCP-1 (CCT, also known as TRiC) is the only, member of the chaperonin family found in the cytosol of eukaryotes. Like, other chaperonins, it assists the folding of newly synthesised proteins., It is, however, unique in its specificity towards only a small subset of, non-native proteins. We determined two crystal structures of mouse, CCTgamma apical domain at 2.2 A and 2.8 A resolution. They reveal a, surface patch facing the inside of the torus that is highly evolutionarily, conserved and specific for the CCTgamma apical domain. This putative, substrate-binding region consists of predominantly positively charged, side-chains. It suggests that the specificity of this apical domain, towards its substrate, partially folded tubulin, is conferred by polar and, electrostatic interactions. The site and nature of substrate interaction, are thus profoundly different between CCT and its eubacterial homologue, GroEL, consistent with their different functions in general versus, specific protein folding assistance. | ||
==About this Structure== | ==About this Structure== | ||
1GML is a | 1GML is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with GOL as [http://en.wikipedia.org/wiki/ligand ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GML OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: tubulin]] | [[Category: tubulin]] | ||
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Revision as of 14:35, 5 November 2007
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CRYSTAL STRUCTURE OF THE MOUSE CCT GAMMA APICAL DOMAIN (TRICLINIC)
OverviewOverview
The chaperonin containing TCP-1 (CCT, also known as TRiC) is the only, member of the chaperonin family found in the cytosol of eukaryotes. Like, other chaperonins, it assists the folding of newly synthesised proteins., It is, however, unique in its specificity towards only a small subset of, non-native proteins. We determined two crystal structures of mouse, CCTgamma apical domain at 2.2 A and 2.8 A resolution. They reveal a, surface patch facing the inside of the torus that is highly evolutionarily, conserved and specific for the CCTgamma apical domain. This putative, substrate-binding region consists of predominantly positively charged, side-chains. It suggests that the specificity of this apical domain, towards its substrate, partially folded tubulin, is conferred by polar and, electrostatic interactions. The site and nature of substrate interaction, are thus profoundly different between CCT and its eubacterial homologue, GroEL, consistent with their different functions in general versus, specific protein folding assistance.
About this StructureAbout this Structure
1GML is a Single protein structure of sequence from Mus musculus with GOL as ligand. Structure known Active Site: AC1. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of the CCTgamma apical domain: implications for substrate binding to the eukaryotic cytosolic chaperonin., Pappenberger G, Wilsher JA, Roe SM, Counsell DJ, Willison KR, Pearl LH, J Mol Biol. 2002 May 17;318(5):1367-79. PMID:12083524
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