PDBsum entry 3lib

Signaling protein

PDB id

3lib

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Contents

			Protein chains

					(+ 4 more) 271 a.a. *

			Metals

					__K ×10

			Waters ×49

* Residue conservation analysis

PDB id:

3lib

Links

Name:

Signaling protein

Title:

Crystal structure of the extracellular domain of the putative histidine kinase mmhk1s-z3

Structure:

Hypothetical sensory transduction histidine kinase. Chain: a, b, c, d, e, f, g, h, i, j. Fragment: extracellular domain (unp residues 32-312). Engineered: yes

Source:

Methanosarcina mazei. Methanosarcina frisia. Organism_taxid: 2209. Strain: dsm 3647. Gene: mm_2965. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Resolution:

2.99Å

R-factor:

0.201

R-free:

0.272

Authors:

Z.Zhang,W.A.Hendrickson

Key ref:

Z.Zhang and W.A.Hendrickson (2010). Structural characterization of the predominant family of histidine kinase sensor domains. J Mol Biol, 400, 335-353. PubMed id: 20435045

Date:

24-Jan-10

Release date:

05-May-10

PROCHECK

	Headers

	References

Protein chains

Q8PSW1 (Q8PSW1_METMA) - histidine kinase from Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)

Seq: Struc:

Seq: Struc:					839 a.a. 271 a.a.

Key:

PfamA domain

Secondary structure

CATH domain



		Enzyme reactions

Enzyme class:

E.C.2.7.13.3 - histidine kinase.

[IntEnz] [ExPASy] [KEGG] [BRENDA]

Reaction:

ATP + protein L-histidine = ADP + protein N-phospho-L-histidine

ATP	+	protein L-histidine	=	ADP	+	protein N-phospho-L-histidine

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

	J Mol Biol 400:335-353 (2010)
PubMed id: 20435045

Structural characterization of the predominant family of histidine kinase sensor domains.
Z.Zhang, W.A.Hendrickson.

ABSTRACT

Histidine kinase receptors are used ubiquitously by bacteria to monitor environmental changes, and they are also prevalent in plants, fungi and other protists. Typical histidine kinase receptors have an extracellular sensor portion to detect the signal, usually a chemical ligand, and an intracellular transmitter portion that includes both the kinase domain itself and the site for histidine phosphorylation. While the kinase domains are highly conserved, sensor domains are diverse. Histidine kinase receptors function as dimers, but the molecular mechanism for signal transduction across cell membranes remains obscure. In this study, eight crystal structures were determined from five sensor domains representative of the most populated family, Family HK1, found in a bioinformatic analysis of predicted sensor domains from transmembrane histidine kinases. Each structure contains an inserted repeat of PhoQ/DcuS/CitA (PDC) domains, and similarity between sequence and structure is correlated across these and other double-PDC sensor proteins. Three of the five sensors crystallize as dimers that appear to be physiologically relevant, and comparisons between ligated-and apo-state structures provide insights into signal transmission. Some HK1-family proteins prove to be sensors for chemotaxis proteins or for diguanylate cyclase receptors, which implies a combinatorial molecular evolution.

Literature references that cite this PDB file's key reference

PubMed id

Reference

20862217

T.E.Edwards, I.Phan, J.Abendroth, S.H.Dieterich, A.Masoudi, W.Guo, S.N.Hewitt, A.Kelley, D.Leibly, M.J.Brittnacher, B.L.Staker, S.I.Miller, W.C.Van Voorhis, P.J.Myler, and L.J.Stewart (2010).
Structure of a Burkholderia pseudomallei trimeric autotransporter adhesin head.

PLoS One, 5, 0.

PDB codes:

3la9 3laa

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. Where a reference describes a PDB structure, the PDB codes are shown on the right.