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PDBsum entry 4zk7
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Protein binding
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PDB id
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4zk7
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Contents |
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(+ 6 more)
117 a.a.
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(+ 5 more)
103 a.a.
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109 a.a.
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PDB id:
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| Name: |
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Protein binding
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Title:
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Crystal structure of rescued two-component self-assembling tetrahedral cage t33-31
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Structure:
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Chorismate mutase. Chain: a, b, c, d, e, f, g, h, i, j, k, l. Fragment: chorismate mutase. Engineered: yes. Mutation: yes. Divalent-cation tolerance protein cuta. Chain: m, n, o, p, q, r, s, t, u, v, w, x. Fragment: divalent cation tolerance protein. Engineered: yes.
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Source:
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Thermus thermophilus (strain hb8 / atcc 27634 / dsm 579). Organism_taxid: 300852. Strain: hb8 / atcc 27634 / dsm 579. Gene: ttha0868. Expressed in: escherichia coli. Expression_system_taxid: 469008. Gene: cuta, ttha1356.
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Resolution:
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3.40Å
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R-factor:
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0.192
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R-free:
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0.239
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Authors:
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Y.Liu,D.Cascio,M.R.Sawaya,J.Bale,M.J.Collazo,R.Park,N.King,D.Baker, T.Yeates
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Key ref:
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J.B.Bale
et al.
(2015).
Structure of a designed tetrahedral protein assembly variant engineered to have improved soluble expression.
Protein Sci,
24,
1695-1701.
PubMed id:
DOI:
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Date:
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30-Apr-15
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Release date:
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29-Jul-15
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PROCHECK
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Headers
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References
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Q5SJY4
(Q5SJY4_THET8) -
Chorismate mutase AroH from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
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Seq:
Struc:
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122 a.a.
117 a.a.*
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Enzyme class 2:
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Chains A, B, C, D, E, F, G, H, I, J, K, L:
E.C.5.4.99.5
- chorismate mutase.
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Pathway:
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Phenylalanine and Tyrosine Biosynthesis
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Reaction:
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chorismate = prephenate
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chorismate
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=
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prephenate
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Enzyme class 3:
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Chains M, N, O, P, Q, R, S, T, U, V, W, X:
E.C.?
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Note, where more than one E.C. class is given (as above), each may
correspond to a different protein domain or, in the case of polyprotein
precursors, to a different mature protein.
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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DOI no:
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Protein Sci
24:1695-1701
(2015)
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PubMed id:
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Structure of a designed tetrahedral protein assembly variant engineered to have improved soluble expression.
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J.B.Bale,
R.U.Park,
Y.Liu,
S.Gonen,
T.Gonen,
D.Cascio,
N.P.King,
T.O.Yeates,
D.Baker.
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ABSTRACT
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We recently reported the development of a computational method for the design of
coassembling multicomponent protein nanomaterials. While four such materials
were validated at high-resolution by X-ray crystallography, low yield of soluble
protein prevented X-ray structure determination of a fifth designed material,
T33-09. Here we report the design and crystal structure of T33-31, a variant of
T33-09 with improved soluble yield resulting from redesign efforts focused on
mutating solvent-exposed side chains to charged amino acids. The structure is
found to match the computational design model with atomic-level accuracy,
providing further validation of the design approach and demonstrating a simple
and potentially general means of improving the yield of designed protein
nanomaterials.
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Links
