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PDBsum entry 3aws
Go to PDB code:
Oxidoreductase/metal transport
PDB id
3aws
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Contents
Protein chains
273 a.a.
78 a.a.
Ligands
NO3
×5
Metals
_CU
×3
Waters
×341
PDB id:
3aws
Links
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CATH
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PDBSWS
PDBePISA
ProSAT
Name:
Oxidoreductase/metal transport
Title:
Crystal structure of streptomyces tyrosinase in a complex with caddie soaked in a cu(ii)-containing solution for 20 hr: occupancy of cu(ii) is low
Structure:
Tyrosinase. Chain: a. Engineered: yes. Melc. Chain: b. Synonym: caddie protein orf378. Engineered: yes
Source:
Streptomyces castaneoglobisporus. Organism_taxid: 79261. Strain: hut 6202. Gene: tyrc. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: orf378.
Resolution:
1.24Å
R-factor:
0.153
R-free:
0.196
Authors:
Y.Matoba,M.Sugiyama
Key ref:
Y.Matoba et al. (2011). A molecular mechanism for copper transportation to tyrosinase that is assisted by a metallochaperone, caddie protein.
J Biol Chem
,
286
, 30219-30231.
PubMed id:
21730070
Date:
26-Mar-11
Release date:
29-Jun-11
PROCHECK
Headers
References
Protein chain
?
Q83WS2
(Q83WS2_9ACTN) - Tyrosinase from Streptomyces castaneoglobisporus
Seq:
Struc:
273 a.a.
273 a.a.
*
Protein chain
?
Q83WS1
(Q83WS1_9ACTN) - MelC from Streptomyces castaneoglobisporus
Seq:
Struc:
126 a.a.
78 a.a.
Key:
PfamA domain
Secondary structure
CATH domain
*
PDB and UniProt seqs differ at 1 residue position (black cross)
Enzyme reactions
Enzyme class:
Chain A:
E.C.1.14.18.1
- tyrosinase.
[IntEnz]
[ExPASy]
[KEGG]
[BRENDA]
Pathway:
Melanin Biosynthesis
Reaction:
1.
L-tyrosine + O2 = L-dopaquinone + H2O
2.
2 L-dopa + O2 = 2 L-dopaquinone + 2 H2O
L-tyrosine
+
O2
=
L-dopaquinone
+
H2O
2 × L-dopa
+
O2
=
2 × L-dopaquinone
+
2 × H2O
Cofactor:
Cu cation
Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
reference
J Biol Chem
286
:30219-30231 (2011)
PubMed id:
21730070
A molecular mechanism for copper transportation to tyrosinase that is assisted by a metallochaperone, caddie protein.
Y.Matoba,
N.Bando,
K.Oda,
M.Noda,
F.Higashikawa,
T.Kumagai,
M.Sugiyama.
ABSTRACT
No abstract given.
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