PDBsum entry 3poa

Peptide binding protein

PDB id

3poa

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Contents

			Protein chain

					96 a.a. *

			Ligands

					THR-ALA-PRO-TPO- GLU-LYS-ILE

			Metals

					_ZN

			Waters ×234

* Residue conservation analysis

PDB id:

3poa

Links

Name:

Peptide binding protein

Title:

Structural and functional analysis of phosphothreonine-dependent fha domain interactions

Structure:

Putative uncharacterized protein tb39.8. Chain: a. Fragment: fha domain. Synonym: rv0020c protein. Engineered: yes. Synthetic phosphopeptide. Chain: b. Engineered: yes

Source:

Mycobacterium tuberculosis. Organism_taxid: 1773. Strain: h37rv. Gene: rv0020c. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Other_details: synthetic

Resolution:

2.01Å

R-factor:

0.182

R-free:

0.237

Authors:

S.Pennell,S.J.Smerdon

Key ref:

S.Pennell et al. (2010). Structural and functional analysis of phosphothreonine-dependent FHA domain interactions. Structure, 18, 1587-1595. PubMed id: 21134638

Date:

22-Nov-10

Release date:

26-Jan-11

PROCHECK

	Headers

	References

Protein chain

P71590 (FHAA_MYCTU) - FHA domain-containing protein FhaA from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

Seq: Struc:

Seq: Struc:					527 a.a. 96 a.a.

Key:

PfamA domain

Secondary structure

CATH domain

	Structure 18:1587-1595 (2010)
PubMed id: 21134638

Structural and functional analysis of phosphothreonine-dependent FHA domain interactions.
S.Pennell, S.Westcott, M.Ortiz-Lombardía, D.Patel, J.Li, T.J.Nott, D.Mohammed, R.S.Buxton, M.B.Yaffe, C.Verma, S.J.Smerdon.

ABSTRACT

No abstract given.

Literature references that cite this PDB file's key reference

PubMed id

Reference

21134632

N.Coquelle, and J.N.Glover (2010).
FHA domain pThr binding specificity: it's all about me.

Structure, 18, 1549-1550.

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.