Structure of the aliphatic sulfonate-binding protein SsuA from Escherichia coli.
Sulfur is an essential component for the biosynthesis of the sulfur-containing amino acids L-methionine and L-cysteine. Under sulfur-starvation conditions, bacteria are capable of scavenging sulfur from sulfur-containing compounds and transporting it across membranes. Here, the crystal structure of the periplasmic aliphatic sulfonate-binding protein SsuA from Escherichia coli is reported at 1.75 A resolution in the substrate-free state. The overall structure of SsuA resembles the structures of other periplasmic binding proteins and contains two globular domains that form a cleft. Comparison with other periplasmic binding proteins revealed that one of the domains has been displaced by a rigid movement of 17 degrees . Interestingly, the tight crystal packing appears to be mediated by a 13-amino-acid tail from the cloning that folds within the cleft of the next monomer.
Beale
John
J
Membrane Protein Laboratory, Diamond Light Source, Harwell Science and Innovation Campus, Oxfordshire OX11 0DE, England.
Lee
Sang Yun
SY
Iwata
So
S
Beis
Konstantinos
K
D002352:Carrier Proteins / Q000737:chemistry*; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000737:chemistry*; D029968:Escherichia coli Proteins / Q000737:chemistry*; D008958:Models, Molecular; D017434:Protein Structure, Tertiary; D040681:Structural Homology, Protein
D002352:Carrier Proteins; D029968:Escherichia coli Proteins; C549628:SsuA protein, E coli
Nat Methods. 2006 Apr;3(4):303-13
16554836
Microbiology (Reading). 1998 Sep;144 ( Pt 9):2555-2561
9782504
J Biol Chem. 1993 May 25;268(15):11348-55
8496186
Nat Protoc. 2008;3(7):1171-9
18600222
Curr Opin Struct Biol. 2004 Aug;14(4):495-504
15313245
Acta Crystallogr A. 1991 Mar 1;47 ( Pt 2):110-9
2025413
Biol Chem. 2009 Nov;390(11):1163-70
19642870
J Biol Chem. 2006 Oct 27;281(43):32534-9
16891315
J Biol Chem. 1997 Sep 12;272(37):23031-6
9287300
Proc Natl Acad Sci U S A. 2006 Jun 27;103(26):9820-5
16777960
Biochemistry. 2002 Apr 23;41(16):5185-92
11955067
Biochemistry. 2003 May 20;42(19):5547-54
12741810
Acta Crystallogr D Biol Crystallogr. 2004 Dec;60(Pt 12 Pt 1):2256-68
15572779
Acta Crystallogr D Biol Crystallogr. 1997 May 1;53(Pt 3):240-55
15299926
J Biol Chem. 2007 Jan 26;282(4):2606-14
17121816
J Biol Chem. 1999 Sep 17;274(38):26639-46
10480865
J Biol Chem. 2008 Nov 21;283(47):32848-59
18779321
Arch Microbiol. 2001 Jul;176(1-2):1-8
11479697
Acta Crystallogr D Biol Crystallogr. 2008 Jan;64(Pt 1):125-32
18094476
Protein J. 2007 Jun;26(4):231-8
17203388
Trends Biochem Sci. 1995 Nov;20(11):478-80
8578593
Acta Crystallogr D Biol Crystallogr. 2004 Dec;60(Pt 12 Pt 1):2126-32
15572765
J Mol Biol. 2002 Nov 29;324(3):457-68
12445781
J Biol Chem. 1999 Oct 8;274(41):29358-65
10506196
J Bacteriol. 1996 Sep;178(18):5438-46
8808933