 |
PDBsum entry 1w31
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
* Residue conservation analysis
|
|
|
|
|
|
PDB id:
|
|
|
|
| Name: |
|
Lyase
|
|
|
Title:
|
|
Yeast 5-aminolaevulinic acid dehydratase 5-hydroxylaevulinic acid complex
|
|
Structure:
|
|
Delta-aminolevulinic acid dehydratase. Chain: a. Synonym: 5-aminolaevulinic acid dehydratase, aladh. Engineered: yes. Other_details: complex with 5-hydroxylaevulinic acid
|
|
Source:
|
|
Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Strain: ns1(jm109/pns1). Expressed in: escherichia coli. Expression_system_taxid: 562
|
|
Biol. unit:
|
|
Octamer (from PDB file)
|
|
Resolution:
|
|
|
1.90Å
|
R-factor:
|
0.190
|
R-free:
|
0.249
|
|
|
Authors:
|
|
P.T.Erskine,L.Coates,R.Newbold,A.A.Brindley,F.Stauffer,G.D.E.Beaven, R.Gill,S.P.Wood,M.J.Warren,J.B.Cooper,P.M.Shoolingin-Jordan,R.Neier
|
Key ref:
|
|
P.T.Erskine
et al.
(2005).
Structure of yeast 5-aminolaevulinic acid dehydratase complexed with the inhibitor 5-hydroxylaevulinic acid.
Acta Crystallogr D Biol Crystallogr,
61,
1222-1226.
PubMed id:
DOI:
|
|
|
Date:
|
|
|
11-Jul-04
|
Release date:
|
23-Aug-05
|
|
|
|
|
|
|
PROCHECK
|
|
|
|
|
|
Headers
|
|
|
|
References
|
|
|
|
|
|
|
|
P05373
(HEM2_YEAST) -
Delta-aminolevulinic acid dehydratase from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
|
|
|
|
Seq:
Struc:
|
|
|
|
342 a.a.
340 a.a.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Key: |
 |
PfamA domain |
|
|
 |
Secondary structure |
|
 |
CATH domain |
|
|
|
|
|
|
|
|
|
|
|
|
|
Enzyme class:
|
|
E.C.4.2.1.24
- porphobilinogen synthase.
|
|
|
|
|
|
|
Pathway:
|
|
Porphyrin Biosynthesis (early stages)
|
|
|
|
|
|
Reaction:
|
|
2 5-aminolevulinate = porphobilinogen + 2 H2O + H+
|
|
|
|
|
|
2
×
5-aminolevulinate
Bound ligand (Het Group name = )
matches with 70.00% similarity
|
=
|
porphobilinogen
|
+
|
2
×
H2O
|
+
|
H(+)
|
|
|
|
|
|
|
|
|
|
Cofactor:
|
|
Zn(2+)
|
|
|
|
|
|
|
|
|
Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
| |
|
|
| |
|
DOI no:
|
Acta Crystallogr D Biol Crystallogr
61:1222-1226
(2005)
|
|
PubMed id:
|
|
|
|
|
|
| |
|
Structure of yeast 5-aminolaevulinic acid dehydratase complexed with the inhibitor 5-hydroxylaevulinic acid.
|
|
P.T.Erskine,
L.Coates,
R.Newbold,
A.A.Brindley,
F.Stauffer,
G.D.Beaven,
R.Gill,
A.Coker,
S.P.Wood,
M.J.Warren,
P.M.Shoolingin-Jordan,
R.Neier,
J.B.Cooper.
|
|
|
|
|
| |
ABSTRACT
|
|
|
|
| |
|
|
The X-ray structure of the enzyme 5-aminolaevulinic acid dehydratase (ALAD) from
yeast complexed with the competitive inhibitor 5-hydroxylaevulinic acid has been
determined at a resolution of 1.9 A. The structure shows that the inhibitor is
bound by a Schiff-base link to one of the invariant active-site lysine residues
(Lys263). The inhibitor appears to bind in two well defined conformations and
the interactions made by it suggest that it is a very close analogue of the
substrate 5-aminolaevulinic acid (ALA).
|
|
|
|
|
|
| |
Selected figure(s)
|
|
|
|
| |
|
|
|
|
|
|
Figure 1.
Figure 1
The reaction catalysed by 5-aminolaevulinic acid dehydratase (ALAD). Two molecules of
5-aminolaevulinic acid (ALA) are condensed to form the pyrrole porphobilinogen (PBG).
|
|
Figure 2.
Figure 2
(a) A ribbon diagram of the TIM-barrel fold of the ALAD monomer with its pronounced
N-terminal arm and two active-site lysines shown in ball-and-stick representation. (b) The
assembly of ALAD monomers (coloured differently) to form dimers and (c) the organization
of the functional ALAD octamer. This figure and others similar were prepared using the
programs MOLSCRIPT (Kraulis, 1991 [Kraulis, P. (1991). J. Appl. Cryst. 24,
946-950.]-[bluearr.gif] ) and BOBSCRIPT (Esnouf, 1997 [Esnouf, R. (1997). J. Mol.
Graph. Model. 15, 132.]-[bluearr.gif] ).
|
|
|
|
|
|
| |
The above figures are
reprinted
by permission from the IUCr:
Acta Crystallogr D Biol Crystallogr
(2005,
61,
1222-1226)
copyright 2005.
|
|
| |
Figures were
selected
by an automated process.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
 |
 |
|
Links
