1lep | pdb_00001lep

THREE-DIMENSIONAL STRUCTURE OF THE IMMUNODOMINANT HEAT-SHOCK PROTEIN CHAPERONIN-10 OF MYCOBACTERIUM LEPRAE

spinqualitylabelsall models 1lep, resolution 3.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1lep is a 7 chain structure with sequence from Mycobacterium leprae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [CH10_MYCLE] Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.[HAMAP-Rule:MF_00580] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Members of the chaperonin-10 (cpn10) protein family, also called heat shock protein 10 and in Escherichia coli GroES, play an important role in ensuring the proper folding of many proteins. The crystal structure of the Mycobacterium leprae cpn10 (Ml-cpn10) oligomer has been elucidated at a resolution of 3.5 angstroms. The architecture of the Ml-cpn10 heptamer resembles a dome with an oculus in its roof. The inner surface of the dome is hydrophilic and highly charged. A flexible region, known to interact with cpn60, extends from the lower rim of the dome. With the structure of a cpn10 heptamer now revealed and the structure of the E. coli GroEL previously known, models of cpn10:cpn60 and GroEL:GroES complexes are proposed. Structure of the heat shock protein chaperonin-10 of Mycobacterium leprae.,Mande SC, Mehra V, Bloom BR, Hol WG Science. 1996 Jan 12;271(5246):203-7. PMID:8539620 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Chaperonin 3D structures

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