1t3o

Solution NMR

Solution structure of CsrA, a bacterial carbon storage regulatory protein

Released:
Source organism: Bacillus subtilis
Entry authors: Koharudin LMI, Georgiou T, Kleanthous C, Geoffrey R, Kaptein R, Boelens R

Function and Biology Details

Reactions catalysed:
L-arginine + H(2)O = L-ornithine + urea
D-galactose + O(2) = D-galacto-hexodialdose + H(2)O(2)
Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates.
Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. Alpha-Casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec; and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also occurs).
ATP + protein L-histidine = ADP + protein N-phospho-L-histidine
Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds in which each of the Xaa can be either Arg or Lys and Yaa can be either Ser or Ala.
Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins
TSAVLQ-|-SGFRK-NH(2) and SGVTFQ-|-GKFKK the two peptides corresponding to the two self-cleavage sites of the SARS 3C-like proteinase are the two most reactive peptide substrates. The enzyme exhibits a strong preference for substrates containing Gln at P1 position and Leu at P2 position.
UDP-N-acetyl-alpha-D-glucosamine = UDP-2-acetamido-2,6-dideoxy-alpha-D-xylo-hex-4-ulose + H(2)O
Selective cleavage of Gln-|-Gly bond in the poliovirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly.
Selective cleavage of Tyr-|-Gly bond in picornavirus polyprotein.
An acyl-[acyl-carrier protein] + NAD(+) = a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADH
2 bilirubin + O(2) = 2 biliverdin + 2 H(2)O
ATP + H(2)O = ADP + phosphate
S-adenosyl-L-methionine + a 5'-(N(7)-methyl 5'-triphosphoguanosine)-(ribonucleotide)-[mRNA] = S-adenosyl-L-homocysteine + a 5'-(N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyl-ribonucleotide)-[mRNA]
NTP + H(2)O = NDP + phosphate
ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + L-tyrosyl-tRNA(Tyr)
ATP + L-glutamate + NH(3) = ADP + phosphate + L-glutamine
2-iminobutanoate + H(2)O = 2-oxobutanoate + NH(3)
AMP + H(2)O = D-ribose 5-phosphate + adenine
ATP + H(2)O + a folded polypeptide = ADP + phosphate + an unfolded polypeptide
2 6,7-dimethyl-8-(1-D-ribityl)lumazine = riboflavin + 4-(1-D-ribitylamino)-5-amino-2,6-dihydroxypyrimidine
Diphosphate + H(2)O = 2 phosphate
ATP + UMP = ADP + UDP
ATP + thymidine = ADP + thymidine 5'-phosphate
4 Fe(2+) + 4 H(+) + O(2) = 4 Fe(3+) + 2 H(2)O
ATP + adenylyl sulfate = ADP + 3'-phosphoadenylyl sulfate
Isocitrate = succinate + glyoxylate
Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
A beta-lactam + H(2)O = a substituted beta-amino acid
4 benzenediol + O(2) = 4 benzosemiquinone + 2 H(2)O
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
(R)-mandelonitrile = cyanide + benzaldehyde
L-asparagine + H(2)O = L-aspartate + NH(3)
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Translational regulator CsrA Chain: A
Molecule details ›
Chain: A
Length: 95 amino acids
Theoretical weight: 10.68 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
UniProt:
  • Canonical: P33911 (Residues: 1-74; Coverage: 100%)
Gene names: BSU35370, csrA, sow, yviG
Sequence domains: Global regulator protein family
Structure domains: Translational regulator CsrA

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: Automatic peak assignment by ARIA; simulated annealing in CNS;
Expression system: Escherichia coli