4ux5

X-ray diffraction
2.4Å resolution

Structure of DNA complex of PCG2

Released:

Function and Biology Details

Reactions catalysed:
L-rhamnonate = 2-dehydro-3-deoxy-L-rhamnonate + H(2)O
5,10-methylenetetrahydrofolate + dUMP = dihydrofolate + dTMP
A carboxylic ester + H(2)O = an alcohol + a carboxylate
ATP + nucleoside diphosphate = ADP + nucleoside triphosphate
Acetyl-CoA + a 2-deoxystreptamine antibiotic = CoA + N(3)-acetyl-2-deoxystreptamine antibiotic
D-ribose 5-phosphate = D-ribulose 5-phosphate
ATP + AMP = 2 ADP
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.
Autocatalytic release of the core protein from the N-terminus of the togavirus structural polyprotein by hydrolysis of a -Trp-|-Ser- bond.
Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides
Hydrolysis of four peptide bonds in the viral precursor polyprotein, commonly with Asp or Glu in the P6 position, Cys or Thr in P1 and Ser or Ala in P1'.
Prephenate = phenylpyruvate + H(2)O + CO(2)
Hydrolyzes glutaminyl bonds, and activity is further restricted by preferences for the amino acids in P6 - P1' that vary with the species of potyvirus, e.g. Glu-Xaa-Xaa-Tyr-Xaa-Gln-|-(Ser or Gly) for the enzyme from tobacco etch virus. The natural substrate is the viral polyprotein, but other proteins and oligopeptides containing the appropriate consensus sequence are also cleaved.
Hydrolyzes a Gly-|-Gly bond at its own C-terminus, commonly in the sequence -Tyr-Xaa-Val-Gly-|-Gly, in the processing of the potyviral polyprotein.
2 glutathione + ROOH = glutathione disulfide + H(2)O + ROH
Nitric oxide + H(2)O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H(+)
ATP + a protein = ADP + a phosphoprotein
Endopeptidase with a preference for cleavage when the P1 position is occupied by Glu-|- and the P1' position is occupied by Gly-|-
Cutin + H(2)O = cutin monomers
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.
NTP + H(2)O = NDP + phosphate
GDP-beta-L-fucose + NADP(+) = GDP-4-dehydro-alpha-D-rhamnose + NADPH
(S)-dihydroorotate + fumarate = orotate + succinate
Selective cleavage of Tyr-|-Gly bond in picornavirus polyprotein.
An aldehyde + NAD(+) + H(2)O = a carboxylate + NADH
Choline = trimethylamine + acetaldehyde
Acetyl-CoA + L-serine = CoA + O-acetyl-L-serine
ATP + H(2)O + H(+)(Side 1) + K(+)(Side 2) = ADP + phosphate + H(+)(Side 2) + K(+)(Side 1)
ATP + H(2)O = ADP + phosphate
Hydrolyzes poly(ADP-D-ribose) at glycosidic (1''-2') linkage of ribose-ribose bond to produce free ADP-D-ribose
(R)-10-hydroxystearate = oleate + H(2)O
Release of N-terminal proline from a peptide.
Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low.
Succinate semialdehyde + NADP(+) + H(2)O = succinate + NADPH
(S)-3-hydroxyacyl-CoA + NAD(+) = 3-oxoacyl-CoA + NADH
(1a) (2R,3S)-3-isopropylmalate = 2-isopropylmaleate + H(2)O
L-histidine-[translation elongation factor 2] + S-adenosyl-L-methionine = 2-((3S)-3-amino-3-carboxypropyl)-L-histidine-[translation elongation factor 2] + S-methyl-5'-thioadenosine
L-leucine + 2-oxoglutarate = 4-methyl-2-oxopentanoate + L-glutamate
Cleavage of peptide bonds with very broad specificity.
D-xylopyranose = D-xylulose
5,10-methylenetetrahydrofolate + glycine + H(2)O = tetrahydrofolate + L-serine
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.
Diphosphate + H(2)O = 2 phosphate
Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides
Endohydrolysis of RNA in RNA/DNA hybrids. Three different cleavage modes: 1. sequence-specific internal cleavage of RNA. Human immunodeficiency virus type 1 and Moloney murine leukemia virus enzymes prefer to cleave the RNA strand one nucleotide away from the RNA-DNA junction. 2. RNA 5'-end directed cleavage 13-19 nucleotides from the RNA end. 3. DNA 3'-end directed cleavage 15-20 nucleotides away from the primer terminus.
5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + NADPH
3'-end directed exonucleolytic cleavage of viral RNA-DNA hybrid
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).
Beta-D-ribopyranose = beta-D-ribofuranose
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)
Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1)

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
2 distinct DNA molecules
Macromolecules (3 distinct):
HTH APSES-type domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 136 amino acids
Theoretical weight: 15.19 KDa
Source organism: Magnaporthe oryzae
UniProt:
  • Canonical: L7I1M8 (Residues: 82-219; Coverage: 17%)
Gene name: OOU_Y34scaffold00628g4
Sequence domains: KilA-N domain
Structure domains: Transcription regulator HTH, APSES-type DNA-binding domain
5'-D(*CP*AP*AP*TP*GP*AP*CP*GP*CP*GP*TP*AP*AP*GP)-3' Chain: C
Molecule details ›
Chain: C
Length: 14 nucleotides
Theoretical weight: 4.31 KDa
Source organism: Candida albicans
Expression system: Not provided
5'-D(*CP*TP*TP*AP*CP*GP*CP*GP*TP*CP*AP*TP*TP*GP)-3' Chain: D
Molecule details ›
Chain: D
Length: 14 nucleotides
Theoretical weight: 4.25 KDa
Source organism: Candida albicans
Expression system: Not provided

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: P4212
Unit cell:
a: 117.36Å b: 117.36Å c: 65.89Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.231 0.228 0.258
Expression system: Not provided