1p83

Solution NMR

NMR STRUCTURE OF 1-25 FRAGMENT OF MYCOBACTERIUM TUBERCULOSIS CPN10

Released:
Source organism: Mycobacterium tuberculosis
Entry authors: Ciutti A, Spiga O, Giannozzi E, Scarselli M, Di Maro D, Calamandrei D, Niccolai N, Bernini A

Function and Biology Details

Reactions catalysed:
5,10-methylenetetrahydrofolate + dUMP = dihydrofolate + dTMP
D-glucarate = 5-dehydro-4-deoxy-D-glucarate + H(2)O
ATP + molybdopterin = diphosphate + adenylyl-molybdopterin
ATP + (R)-pantoate + beta-alanine = AMP + diphosphate + (R)-pantothenate
UMP + diphosphate = uracil + 5-phospho-alpha-D-ribose 1-diphosphate
Purine deoxynucleoside + phosphate = purine + 2'-deoxy-alpha-D-ribose 1-phosphate
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.
ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate
Trans,octacis-decaprenylphospho-beta-D-ribofuranose + FAD = trans,octacis-decaprenylphospho-beta-D-erythro-pentofuranosid-2-ulose + FADH(2)
ATP + H(2)O = ADP + phosphate
7,8-dihydroneopterin + O(2) = 7,8-dihydroxanthopterin + formate + glycolaldehyde
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate = anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
7,8-dihydroneopterin = 6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde
N(2)-acetyl-L-ornithine + L-glutamate = L-ornithine + N-acetyl-L-glutamate
Selective cleavage of Tyr-|-Gly bond in picornavirus polyprotein.
O-phospho-L-serine + [CysO sulfur-carrier protein]-Gly-NH-CH(2)-C(O)SH = [CysO sulfur-carrier protein]-Gly-NH-CH(2)-C(O)-S-L-cysteine + phosphate
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
Pyridoxamine 5'-phosphate + H(2)O + O(2) = pyridoxal 5'-phosphate + NH(3) + H(2)O(2)
ATP + succinate + CoA = ADP + phosphate + succinyl-CoA
NTP + H(2)O = NDP + phosphate
7,8-dihydroneopterin = 7,8-dihydromonapterin
2 superoxide + 2 H(+) = O(2) + H(2)O(2)
Acts on substrates that are at least partially unfolded. The cleavage site P1 residue is normally between a pair of hydrophobic residues, such as Val-|-Val
ATP + H(2)O + a folded polypeptide = ADP + phosphate + an unfolded polypeptide
Cleavage of peptide bonds with very broad specificity.
Carbamoyl phosphate + L-ornithine = phosphate + L-citrulline
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.
4-phosphonooxy-L-threonine + 2-oxoglutarate = (3R)-3-hydroxy-2-oxo-4-phosphonooxybutanoate + L-glutamate
5,10-methylenetetrahydrofolate + dUMP + NADPH = dTMP + tetrahydrofolate + NADP(+)
ATP + NAD(+) = ADP + NADP(+)
Aceneneuramate = N-acetyl-D-mannosamine + pyruvate
Isocitrate = succinate + glyoxylate
Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.
2-C-methyl-D-erythritol 4-phosphate + NADP(+) = 1-deoxy-D-xylulose 5-phosphate + NADPH
A beta-lactam + H(2)O = a substituted beta-amino acid
The C-O-P bond 3' to the apurinic or apyrimidinic site in DNA is broken by a beta-elimination reaction, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate
4 benzenediol + O(2) = 4 benzosemiquinone + 2 H(2)O
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
Chorismate = prephenate
ATP + [DNA-directed RNA polymerase] = ADP + [DNA-directed RNA polymerase] phosphate
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
10 kDa chaperonin Chain: A
Molecule details ›
Chain: A
Length: 25 amino acids
Theoretical weight: 2.69 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Not provided
UniProt:
  • Canonical: P9WPE5 (Residues: 2-26; Coverage: 25%)
Gene names: MTCY78.11, Rv3418c, cpn10, groES, groS, mopB

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: molecular dynamics
Expression system: Not provided