PDBsum entry: 1jkm

Serine hydrolase

PDB-id: 1jkm

Asymmetric unit

Contents

Description

Header details

Header records

References

PROCHECK

Protein chains

358 a.a. *

Waters ×531

* Residue conservation analysis

Tools

Clefts Calculation

Biological unit*, tetramer
(*as deduced by PQS)

PDB id:

1jkm

Name:

Serine hydrolase

Title:

Brefeldin a esterase, a bacterial homologue of human hormone sensitive lipase

Structure:

Brefeldin a esterase. Chain: a, b. Engineered: yes

Source:

Bacillus subtilis. Organism_taxid: 1423. Cell_line: 293. Expressed in: escherichia coli. Expression_system_taxid: 562.

Biological unit:

Tetramer (from PQS)

UniProt:

Chains A, B: O68884 (O68884_BACSU)

Seq:

Struc:

Seq:

372 a.a.

Struc:

358 a.a.*

Key:	PfamA domain	PfamB domain
Secondary structure	CATH domain

* PDB and UniProt seqs differ at 1 residue position (black cross)

Resolution:

1.85Å

R-factor:

0.170

R-free:

0.206

Authors:

Y.Wei,A.J.Contreras,P.Sheffield,T.Osterlund,U.Derewenda, U.O.Matern,Z.S.Derewenda

Key ref:

Y.Wei et al. (1999). Crystal structure of brefeldin A esterase, a bacterial homolog of the mammalian hormone-sensitive lipase.. Nat Struct Biol, 6, 340-345. [PubMed id: 10201402] [DOI: 10.1038/7576]

Date:

04-Feb-98

Release date:

16-Feb-99

Quick_links

Procheck

Clefts

Surface

Key reference

DOI no: 10.1038/7576

Nat Struct Biol 6:340-345 (1999)

PubMed id: 10201402

Crystal structure of brefeldin A esterase, a bacterial homolog of the mammalian hormone-sensitive lipase.

Y.Wei, J.A.Contreras, P.Sheffield, T.Osterlund, U.Derewenda, R.E.Kneusel, U.Matern, C.Holm, Z.S.Derewenda.

ABSTRACT

Brefeldin A esterase (BFAE), a detoxifying enzyme isolated from Bacillus subtilis, hydrolyzes and inactivates BFA, a potent fungal inhibitor of intracellular vesicle-dependent secretory transport and poliovirus RNA replication. We have solved the crystal structure of BFAE and we discovered that the previously reported amino acid sequence was in serious error due to frame shifts in the cDNA sequence. The correct sequence, inferred from the experimentally phased electron density map, revealed that BFAE is a homolog of the mammalian hormone sensitive lipase (HSL). It is a canonical alpha/beta hydrolase with two insertions forming the substrate binding pocket. The enzyme contains a lipase-like catalytic triad, Ser 202, Asp 308 and His 338, consistent with mutational studies that implicate the homologous Ser 424, Asp 693 and His 723 in the catalytic triad in human HSL.

Selected figure(s)

Figure 2.
Figure 2. green depicts the N-terminal fragment containing two helices( 1, 30−41 and 2, 56−78); the central -pleated sheet is shown in yellow ( 1, 89−98; 2, 102−111; 3, 119−127; 4, 151−158; 5, 194−201; 6, 226−231; 7, 299−306; 8, 327−334) while the -helices of the core fragment are shown in pale blue ( 3, 137−149; 4, 171−188; 5, 203−218; 9, 310−324; 10, 349−370); the red color denotes an insertion in the fifth connecting loop on the carboxyl edge of the sheet ( 6, 241−248; 7, 262−273; 8, 290−295); the three active site residues are shown in full. b, A schematic representation of the fold showing the canonical / hydrolase core. The color scheme corresponds to that in (a). c, C trace in stereo.

Figure 3.
Figure 3. a, The vicinity of the catalytic site in BFAE. The key residues are labeled and the hydrogen bonds are shown using broken lines. b, A model of the catalytic site in HSL based on the BFAE structure.

The above figures are reprinted by permission from Macmillan Publishers Ltd: Nat Struct Biol (1999, 6, 340-345) copyright 1999.

Figures were selected by an automated process.