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PDBsum entry 2pl2
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Protein binding
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PDB id
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2pl2
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Contents |
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* Residue conservation analysis
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Mol Cells
24:27-36
(2007)
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PubMed id:
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Crystal structure of TTC0263, a thermophilic TPR protein from Thermus thermophilus HB27.
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H.Lim,
K.Kim,
D.Han,
J.Oh,
Y.Kim.
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ABSTRACT
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The hypothetical protein TTC0263 of Thermus thermophilus HB27 is a thermophilic
tetratricopeptide repeat (TPR)-containing protein. In the present study, the TPR
region (residues 26-230) was resolved at 2.5 A with R-factors of R/Rfree =
23.6%/28.6%. TTC0263 consists of 11 helices that form five TPR units. Uniquely,
it contains one atypical "extended" TPR (eTPR) unit. This comprises extended
helical residues near the loop region of TTC0263, such that the helical length
of eTPR is longer than that of the canonical TPR sequence. In addition, the
hybrid TPR domain of TTC0263 possesses oligomer-forming characteristics. TPR
domains are generally involved in forming multi-subunit complexes by interacting
with each other or with other subunit proteins. The dynamic structure of TTC0263
described here goes some way to explaining how TPR domains mediate the formation
of multi-subunit complexes.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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S.Park,
and
R.L.Ely
(2008).
Candidate stress genes of Nitrosomonas europaea for monitoring inhibition of nitrification by heavy metals.
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Appl Environ Microbiol,
74,
5475-5482.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
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