PDBsum entry 2ftk

Transferase

PDB id

2ftk

Loading ...

Contents

			Protein chains

					181 a.a. *


					119 a.a. *

			Metals

					_MG ×4

* Residue conservation analysis

PDB id:

2ftk

Links

Name:

Transferase

Title:

Berylloflouride spo0f complex with spo0b

Structure:

Sporulation initiation phosphotransferase b. Chain: a, b, c, d. Synonym: stage 0 sporulation protein b. Engineered: yes. Sporulation initiation phosphotransferase f. Chain: e, f, g, h. Synonym: stage 0 sporulation protein f. Engineered: yes. Mutation: yes

Source:

Bacillus subtilis. Organism_taxid: 1423. Gene: spo0b, spo0d. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: spo0f. Expression_system_taxid: 562

Biol. unit:

Tetramer (from PQS)

Resolution:

3.05Å

R-factor:

0.232

R-free:

0.282

Authors:

K.I.Varughese

Key ref:

K.I.Varughese et al. (2006). The crystal structure of beryllofluoride Spo0F in complex with the phosphotransferase Spo0B represents a phosphotransfer pretransition state. J Bacteriol, 188, 4970-4977. PubMed id: 16788205

Date:

24-Jan-06

Release date:

18-Jul-06

PROCHECK

	Headers

	References

Protein chains

P06535 (SP0B_BACSU) - Sporulation initiation phosphotransferase B from Bacillus subtilis (strain 168)

Seq: Struc:					192 a.a. 181 a.a.

Protein chains

P06628 (SP0F_BACSU) - Sporulation initiation phosphotransferase F from Bacillus subtilis (strain 168)

Seq: Struc:					124 a.a. 119 a.a.*

Key:

PfamA domain

Secondary structure

CATH domain

* PDB and UniProt seqs differ at 2 residue positions (black crosses)



		Enzyme reactions

Enzyme class:

Chains A, B, C, D, E, F, G, H: E.C.2.7.-.-

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

	J Bacteriol 188:4970-4977 (2006)
PubMed id: 16788205

The crystal structure of beryllofluoride Spo0F in complex with the phosphotransferase Spo0B represents a phosphotransfer pretransition state.
K.I.Varughese, I.Tsigelny, H.Zhao.

ABSTRACT

A number of regulatory circuits in biological systems function through the exchange of phosphoryl groups from one protein to another. Spo0F and Spo0B are components of a phosphorelay that control sporulation in the bacterium Bacillus subtilis through the exchange of a phosphoryl group. Using beryllofluoride as a mimic for phosphorylation, we trapped the interaction of the phosphorylated Spo0F with Spo0B in the crystal lattice. The transition state of phosphoryl transfer continues to be a highly debated issue, as to whether it is associative or dissociative in nature. The geometry of Spo0F binding to Spo0B favors an associative mechanism for phosphoryl transfer. In order to visualize the autophosphorylation of the histidine kinase, KinA, and the subsequent phosphoryl transfer to Spo0F, we generated in silico models representing these reaction steps.

Literature references that cite this PDB file's key reference

PubMed id

Reference

21481780

K.Schmöe, V.V.Rogov, N.Y.Rogova, F.Löhr, P.Güntert, F.Bernhard, and V.Dötsch (2011).
Structural Insights into Rcs Phosphotransfer: The Newly Identified RcsD-ABL Domain Enhances Interaction with the Response Regulator RcsB.

Structure, 19, 577-587.

PDB code:

2kx7

21346797

V.Parashar, N.Mirouze, D.A.Dubnau, and M.B.Neiditch (2011).
Structural basis of response regulator dephosphorylation by rap phosphatases.

PLoS Biol, 9, e1000589.

PDB code:

3q15

20161720

C.H.Bell, S.L.Porter, A.Strawson, D.I.Stuart, and J.P.Armitage (2010).
Using structural information to change the phosphotransfer specificity of a two-component chemotaxis signalling complex.

PLoS Biol, 8, e1000306.

PDB codes:

3kyi 3kyj

20133181

H.Szurmant, and J.A.Hoch (2010).
Interaction fidelity in two-component signaling.

Curr Opin Microbiol, 13, 190-197.

20226790

R.D.Hills, S.V.Kathuria, L.A.Wallace, I.J.Day, C.L.Brooks, and C.R.Matthews (2010).
Topological frustration in beta alpha-repeat proteins: sequence diversity modulates the conserved folding mechanisms of alpha/beta/alpha sandwich proteins.

J Mol Biol, 398, 332-350.

20080618

Y.Pazy, M.A.Motaleb, M.T.Guarnieri, N.W.Charon, R.Zhao, and R.E.Silversmith (2010).
Identical phosphatase mechanisms achieved through distinct modes of binding phosphoprotein substrate.

Proc Natl Acad Sci U S A, 107, 1924-1929.

PDB code:

3hzh

19503843

A.Chakicherla, C.L.Ecale Zhou, M.L.Dang, V.Rodriguez, J.N.Hansen, and A.Zemla (2009).
SpaK/SpaR two-component system characterized by a structure-driven domain-fusion method and in vitro phosphorylation studies.

PLoS Comput Biol, 5, e1000401.

20018738

A.Schug, M.Weigt, J.N.Onuchic, T.Hwa, and H.Szurmant (2009).
High-resolution protein complexes from integrating genomic information with molecular simulation.

Proc Natl Acad Sci U S A, 106, 22124-22129.

18956421

N.Ni, M.Li, J.Wang, and B.Wang (2009).
Inhibitors and antagonists of bacterial quorum sensing.

Med Res Rev, 29, 65.

19800110

P.Casino, V.Rubio, and A.Marina (2009).
Structural insight into partner specificity and phosphoryl transfer in two-component signal transduction.

Cell, 139, 325-336.

PDB codes:

3dge 3dgf 3gl9

19561131

P.Eswaramoorthy, T.Guo, and M.Fujita (2009).
In vivo domain-based functional analysis of the major sporulation sensor kinase, KinA, in Bacillus subtilis.

J Bacteriol, 191, 5358-5368.

19399227

R.D.Hills, and C.L.Brooks (2009).
Insights from coarse-grained gō models for protein folding and dynamics.

Int J Mol Sci, 10, 889-905.

19246748

R.Shrivastava, A.K.Ghosh, and A.K.Das (2009).
Intra- and intermolecular domain interactions among novel two-component system proteins coded by Rv0600c, Rv0601c and Rv0602c of Mycobacterium tuberculosis.

Microbiology, 155, 772-779.

19836334

S.Yamada, H.Sugimoto, M.Kobayashi, A.Ohno, H.Nakamura, and Y.Shiro (2009).
Structure of PAS-linked histidine kinase and the response regulator complex.

Structure, 17, 1333-1344.

PDB codes:

3a0r 3a0s 3a0t 3a0u 3a0v 3a0w 3a0x 3a0y 3a0z 3a10

18214466

C.Neylon (2008).
Small angle neutron and X-ray scattering in structural biology: recent examples from the literature.

Eur Biophys J, 37, 531-541.

18353359

G.Wisedchaisri, M.Wu, D.R.Sherman, and W.G.Hol (2008).
Crystal structures of the response regulator DosR from Mycobacterium tuberculosis suggest a helix rearrangement mechanism for phosphorylation activation.

J Mol Biol, 378, 227-242.

PDB codes:

3c3w 3c57

18588317

H.Szurmant, B.G.Bobay, R.A.White, D.M.Sullivan, R.J.Thompson, T.Hwa, J.A.Hoch, and J.Cavanagh (2008).
Co-evolving motions at protein-protein interfaces of two-component signaling systems identified by covariance analysis.

Biochemistry, 47, 7782-7784.

18557815

S.A.Thomas, J.A.Brewster, and R.B.Bourret (2008).
Two variable active site residues modulate response regulator phosphoryl group stability.

Mol Microbiol, 69, 453-465.

18076904

X.Zhao, D.M.Copeland, A.S.Soares, and A.H.West (2008).
Crystal structure of a complex between the phosphorelay protein YPD1 and the response regulator domain of SLN1 bound to a phosphoryl analog.

J Mol Biol, 375, 1141-1151.

PDB code:

2r25

17322531

T.Gao, X.Zhang, N.B.Ivleva, S.S.Golden, and A.LiWang (2007).
NMR structure of the pseudo-receiver domain of CikA.

Protein Sci, 16, 465-475.

PDB code:

2j48

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 code is shown on the right.