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PDBsum entry 3m6c
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Contents |
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* Residue conservation analysis
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PDB id:
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Chaperone
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Title:
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Crystal structure of mycobacterium tuberculosis groel1 apical domain
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Structure:
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60 kda chaperonin 1. Chain: a. Fragment: unp residues 184-377. Synonym: protein cpn60-1, groel protein 1. Engineered: yes
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Source:
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Mycobacterium tuberculosis. Organism_taxid: 83332. Strain: h37rv. Gene: groel-1, groel1, grol1, mt3526, mtcy78.12, rv3417c. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Resolution:
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2.20Å
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R-factor:
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0.210
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R-free:
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0.232
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Authors:
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F.T.F.Tsai,B.Sielaff,K.Lee
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Key ref:
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B.Sielaff
et al.
(2011).
Structural and functional conservation of Mycobacterium tuberculosis GroEL paralogs suggests that GroEL1 Is a chaperonin.
J Mol Biol,
405,
831-839.
PubMed id:
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Date:
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15-Mar-10
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Release date:
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08-Dec-10
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PROCHECK
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Headers
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References
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P9WPE9
(CH601_MYCTU) -
Chaperonin GroEL 1 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
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Seq:
Struc:
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539 a.a.
194 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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Enzyme class:
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E.C.5.6.1.7
- chaperonin ATPase.
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Reaction:
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ATP + H2O + a folded polypeptide = ADP + phosphate + an unfolded polypeptide
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ATP
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+
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H2O
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+
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folded polypeptide
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=
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ADP
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+
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phosphate
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+
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unfolded polypeptide
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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J Mol Biol
405:831-839
(2011)
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PubMed id:
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Structural and functional conservation of Mycobacterium tuberculosis GroEL paralogs suggests that GroEL1 Is a chaperonin.
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B.Sielaff,
K.S.Lee,
F.T.Tsai.
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ABSTRACT
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Links
