PDBsum entry 2qla

Electron transport

PDB id

2qla

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Contents

			Protein chains

					106 a.a. *

			Ligands

					HEM ×4

			Metals

					_ZN ×4

			Waters ×31

* Residue conservation analysis

PDB id:

2qla

Links

Name:

Electron transport

Title:

Crystal structure of a 16-helix bundle architecture produced by the zinc-mediated self assembly of four cytochrome cb562 molecules

Structure:

Soluble cytochrome b562. Chain: a, b, c, d. Synonym: cytochrome b-562. Engineered: yes. Mutation: yes

Source:

Escherichia coli. Organism_taxid: 562. Gene: cybc. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

2.90Å

R-factor:

0.248

R-free:

0.295

Authors:

F.A.Tezcan,E.N.Salgado,J.Faraone-Mennella

Key ref:

E.N.Salgado et al. (2007). Controlling protein-protein interactions through metal coordination: assembly of a 16-helix bundle protein. J Am Chem Soc, 129, 13374-13375. PubMed id: 17929927

Date:

12-Jul-07

Release date:

06-Nov-07

PROCHECK

	Headers

	References

Protein chains

P0ABE7 (C562_ECOLX) - Soluble cytochrome b562 from Escherichia coli

Seq: Struc:					128 a.a. 106 a.a.*

Key:

PfamA domain

Secondary structure

CATH domain

* PDB and UniProt seqs differ at 5 residue positions (black crosses)

	J Am Chem Soc 129:13374-13375 (2007)
PubMed id: 17929927

Controlling protein-protein interactions through metal coordination: assembly of a 16-helix bundle protein.
E.N.Salgado, J.Faraone-Mennella, F.A.Tezcan.

ABSTRACT

No abstract given.

Literature references that cite this PDB file's key reference

PubMed id

Reference

21331408

C.M.Yang (2011).
Biometal binding-site mimicry with modular, hetero-bifunctionally modified architecture encompassing a Trp/His motif: insights into spatiotemporal noncovalent interactions from a comparative spectroscopic study.

Dalton Trans, 40, 3008-3027.

20189099

B.Höcker (2010).
Metals make proteins stick.

Chem Biol, 17, 103-104.

20669189

C.M.Yang, and J.Zhang (2010).
Insights into intramolecular Trp and His side-chain orientation and stereospecific π interactions surrounding metal centers: an investigation using protein metal-site mimicry in solution.

Chemistry, 16, 10854-10865.

20192262

E.N.Salgado, R.J.Radford, and F.A.Tezcan (2010).
Metal-directed protein self-assembly.

Acc Chem Res, 43, 661-672.

20080561

E.N.Salgado, X.I.Ambroggio, J.D.Brodin, R.A.Lewis, B.Kuhlman, and F.A.Tezcan (2010).
Metal templated design of protein interfaces.

Proc Natl Acad Sci U S A, 107, 1827-1832.

PDB codes:

3hni 3hnj 3hnk 3hnl

20377257

R.J.Radford, P.C.Nguyen, T.B.Ditri, J.S.Figueroa, and F.A.Tezcan (2010).
Controlled protein dimerization through hybrid coordination motifs.

Inorg Chem, 49, 4362-4369.

PDB code:

3l1m

19267481

E.N.Salgado, R.A.Lewis, S.Mossin, A.L.Rheingold, and F.A.Tezcan (2009).
Control of protein oligomerization symmetry by metal coordination: C2 and C3 symmetrical assemblies through Cu(II) and Ni(II) coordination.

Inorg Chem, 48, 2726-2728.

PDB codes:

3de8 3de9

19834935

P.B.Crowley, P.M.Matias, A.R.Khan, M.Roessle, and D.I.Svergun (2009).
Metal-mediated self-assembly of a beta-sandwich protein.

Chemistry, 15, 12672-12680.

PDB codes:

2w88 2w8c

19527025

R.J.Radford, and F.A.Tezcan (2009).
A superprotein triangle driven by nickel(II) coordination: exploiting non-natural metal ligands in protein self-assembly.

J Am Chem Soc, 131, 9136-9137.

PDB codes:

3foo 3fop

19675646

Y.Lu, N.Yeung, N.Sieracki, and N.M.Marshall (2009).
Design of functional metalloproteins.

Nature, 460, 855-862.

18422313

E.N.Salgado, R.A.Lewis, J.Faraone-Mennella, and F.A.Tezcan (2008).
Metal-mediated self-assembly of protein superstructures: influence of secondary interactions on protein oligomerization and aggregation.

J Am Chem Soc, 130, 6082-6084.

PDB codes:

3c62 3c63

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.