PDBsum entry 1a24

Oxidoreductase

PDB id

1a24

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Contents

			Protein chain

					189 a.a. *

* Residue conservation analysis

PDB id:

1a24

Links

Name:

Oxidoreductase

Title:

Solution nmr structure of reduced dsba from escherichia coli, family of 20 structures

Structure:

Dsba. Chain: a. Engineered: yes

Source:

Escherichia coli. Organism_taxid: 562. Strain: thz2. Cellular_location: periplasm. Gene: dsba. Expressed in: escherichia coli. Expression_system_taxid: 562.

NMR struc:

20 models

Authors:

H.J.Schirra,C.Renner,M.Czisch,M.Huber-Wunderlich,T.A.Holak, R.Glockshuber

Key ref:

H.J.Schirra et al. (1998). Structure of reduced DsbA from Escherichia coli in solution. Biochemistry, 37, 6263-6276. PubMed id: 9572841 DOI: 10.1021/bi980136y

Date:

15-Jan-98

Release date:

16-Sep-98

PROCHECK

	Headers

	References

Protein chain

P0AEG4 (DSBA_ECOLI) - Thiol:disulfide interchange protein DsbA from Escherichia coli (strain K12)

Seq: Struc:					208 a.a. 189 a.a.

Key:

PfamA domain

Secondary structure

CATH domain



		Enzyme reactions

Enzyme class:

E.C.?

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

DOI no: 10.1021/bi980136y	Biochemistry 37:6263-6276 (1998)
PubMed id: 9572841

Structure of reduced DsbA from Escherichia coli in solution.
H.J.Schirra, C.Renner, M.Czisch, M.Huber-Wunderlich, T.A.Holak, R.Glockshuber.

ABSTRACT

The three-dimensional structure of reduced DsbA from Escherichia coli in aqueous solution has been determined by nuclear magnetic resonance (NMR) spectroscopy and is compared with the crystal structure of oxidized DsbA [Guddat, L. W., Bardwell, J. C. A., Zander, T., and Martin, J. L. (1997) Protein Sci. 6, 1148-1156]. DsbA is a monomeric 21 kDa protein which consists of 189 residues and is required for disulfide bond formation in the periplasm of E. coli. On the basis of sequence-specific 1H NMR assignments, 1664 nuclear Overhauser enhancement distance constraints, 118 hydrogen bond distance constraints, and 293 dihedral angle constraints were obtained as the input for the structure calculations by simulated annealing with the program X-PLOR. The enzyme is made up of two domains. The catalytic domain has a thioredoxin-like fold with a five-stranded beta-sheet and three alpha-helices, and the second domain consists of four alpha-helices and is inserted into the thioredoxin motif. The active site between Cys30 and Cys33 is located at the N terminus of the first alpha-helix in the thioredoxin-like domain. The solution structure of reduced DsbA is rather similar to the crystal structure of the oxidized enzyme but exhibits a different relative orientation of both domains. In addition, the conformations of the active site and a loop between strand beta5 and helix alpha7 are slightly different. These structural differences may reflect important functional requirements in the reaction cycle of DsbA as they appear to facilitate the release of oxidized polypeptides from reduced DsbA. The extremely low pKa value of the nucleophilic active site thiol of Cys30 in reduced DsbA is most likely caused by its interactions with the dipole of the active site helix and the side chain of His32, as no other charged residues are located next to the sulfur atom of Cys30 in the solution structure.

Literature references that cite this PDB file's key reference

PubMed id

Reference

19953303

L.J.Sperling, A.J.Nieuwkoop, A.S.Lipton, D.A.Berthold, and C.M.Rienstra (2010).
High resolution NMR spectroscopy of nanocrystalline proteins at ultra-high magnetic field.

J Biomol NMR, 46, 149-155.

20455034

T.Collins, M.Matzapetakis, and H.Santos (2010).
Backbone and side chain 1H, 15N and 13C assignments for a thiol-disulphide oxidoreductase from the Antarctic bacterium Pseudoalteromonas haloplanktis TAC125.

Biomol NMR Assign, 4, 151-154.

19820233

D.Pantoja-Uceda, J.L.Arolas, F.X.Aviles, J.Santoro, S.Ventura, and C.P.Sommerhoff (2009).
Deciphering the structural basis that guides the oxidative folding of leech-derived tryptase inhibitor.

J Biol Chem, 284, 35612-35620.

PDB codes:

2kmo 2kmp 2kmq 2kmr

19389711

J.J.Paxman, N.A.Borg, J.Horne, P.E.Thompson, Y.Chin, P.Sharma, J.S.Simpson, J.Wielens, S.Piek, C.M.Kahler, H.Sakellaris, M.Pearce, S.P.Bottomley, J.Rossjohn, and M.J.Scanlon (2009).
The structure of the bacterial oxidoreductase enzyme DsbA in complex with a peptide reveals a basis for substrate specificity in the catalytic cycle of DsbA enzymes.

J Biol Chem, 284, 17835-17845.

PDB code:

3dks

16586531

A.T.Carvalho, P.A.Fernandes, and M.J.Ramos (2006).
Determination of the DeltapKa between the active site cysteines of thioredoxin and DsbA.

J Comput Chem, 27, 966-975.

16815710

C.W.Gruber, M.Cemazar, B.Heras, J.L.Martin, and D.J.Craik (2006).
Protein disulfide isomerase: the structure of oxidative folding.

Trends Biochem Sci, 31, 455-464.

16446111

J.Messens, and J.F.Collet (2006).
Pathways of disulfide bond formation in Escherichia coli.

Int J Biochem Cell Biol, 38, 1050-1062.

16418167

X.Zhang, Y.Hu, X.Guo, E.Lescop, Y.Li, B.Xia, and C.Jin (2006).
The Bacillus subtilis YkuV is a thiol:disulfide oxidoreductase revealed by its redox structures and activity.

J Biol Chem, 281, 8296-8304.

PDB codes:

2b5x 2b5y

14747707

B.A.Manjasetty, J.Hennecke, R.Glockshuber, and U.Heinemann (2004).
Structure of circularly permuted DsbA(Q100T99): preserved global fold and local structural adjustments.

Acta Crystallogr D Biol Crystallogr, 60, 304-309.

PDB code:

1un2

15340164

E.Moutevelis, and J.Warwicker (2004).
Prediction of pKa and redox properties in the thioredoxin superfamily.

Protein Sci, 13, 2744-2752.

12524212

H.Kadokura, F.Katzen, and J.Beckwith (2003).
Protein disulfide bond formation in prokaryotes.

Annu Rev Biochem, 72, 111-135.

13678522

J.Blank, T.Kupke, E.Lowe, P.Barth, R.B.Freedman, and L.W.Ruddock (2003).
The influence of His94 and Pro149 in modulating the activity of V. cholerae DsbA.

Antioxid Redox Signal, 5, 359-366.

12493830

J.J.Miranda (2003).
Position-dependent interactions between cysteine residues and the helix dipole.

Protein Sci, 12, 73-81.

12193604

B.Philipps, and R.Glockshuber (2002).
Randomization of the entire active-site helix alpha 1 of the thiol-disulfide oxidoreductase DsbA from Escherichia coli.

J Biol Chem, 277, 43050-43057.

12070313

F.Vinci, J.Couprie, P.Pucci, E.Quéméneur, and M.Moutiez (2002).
Description of the topographical changes associated to the different stages of the DsbA catalytic cycle.

Protein Sci, 11, 1600-1612.

11544348

D.Ritz, and J.Beckwith (2001).
Roles of thiol-redox pathways in bacteria.

Annu Rev Microbiol, 55, 21-48.

10828992

J.Couprie, F.Vinci, C.Dugave, E.Quéméneur, and M.Moutiez (2000).
Investigation of the DsbA mechanism through the synthesis and analysis of an irreversible enzyme-ligand complex.

Biochemistry, 39, 6732-6742.

10633106

L.Debarbieux, and J.Beckwith (2000).
On the functional interchangeability, oxidant versus reductant, of members of the thioredoxin superfamily.

J Bacteriol, 182, 723-727.

10584070

A.Sillen, J.Hennecke, D.Roethlisberger, R.Glockshuber, and Y.Engelborghs (1999).
Fluorescence quenching in the DsbA protein from Escherichia coli: complete picture of the excited-state energy pathway and evidence for the reshuffling dynamics of the microstates of tryptophan.

Proteins, 37, 253-263.

10092865

S.A.Guerrero, L.Flohé, H.M.Kalisz, M.Montemartini, E.Nogoceke, H.J.Hecht, P.Steinert, and M.Singh (1999).
Sequence, heterologous expression and functional characterization of tryparedoxin1 from Crithidia fasciculata.

Eur J Biochem, 259, 789-794.

9860875

J.Hennecke, and R.Glockshuber (1998).
Conversion of a catalytic into a structural disulfide bond by circular permutation.

Biochemistry, 37, 17590-17597.

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.