PDBsum entry 3dnm

Hydrolase

PDB id: 3dnm

Contents

Protein chains

297 a.a. *

Ligands

BME ×4

SO4 ×14

Waters ×204

* Residue conservation analysis

PDB id:

3dnm

Name:

Hydrolase

Title:

Crystal structure hormone-sensitive lipase from a metagenome library

Structure:

Esterase/lipase. Chain: a, b, c, d. Engineered: yes

Source:

Uncultured bacterium. Organism_taxid: 77133. Gene: este7. Expressed in: escherichia coli. Expression_system_taxid: 562. Other_details: this protein was purified from metagenome library(soil uncultured bacteria)

Resolution:

2.80Å R-factor: 0.233 R-free: 0.282

Authors:

K.Y.Hwang,K.H.Nam

Key ref:

K.H.Nam et al. (2009). Structural and functional analysis of a novel hormone-sensitive lipase from a metagenome library. Proteins, 74, 1036-1040. PubMed id: 19089974 DOI: 10.1002/prot.22313

Date:

02-Jul-08 Release date: 13-Jan-09

Protein chains

Q0GMU1  (Q0GMU1_9BACT) -  Esterase/lipase from uncultured bacterium

Seq: 309 a.a.

Struc: 297 a.a.

Enzyme reactions

• Enzyme class: E.C.3.1.1.- - ?????

DOI no: 10.1002/prot.22313

Proteins 74:1036-1040 (2009)

PubMed id: 19089974

Structural and functional analysis of a novel hormone-sensitive lipase from a metagenome library.

K.H.Nam, M.Y.Kim, S.J.Kim, A.Priyadarshi, S.T.Kwon, B.S.Koo, S.H.Yoon, K.Y.Hwang.

ABSTRACT

No abstract given.

Selected figure(s)

Figure 1.
Figure 1. Biological and structural analysis of EstE7. (a) Relative activity of recombinant EstE7 toward p-nitrophenyl esters. Esterase activity was determined photometrically in a 50 mM Tris-HCl buffer (pH 7.5) using various p-nitrophenyl esters as substrates. (b) The EstE7 monomer structure has two domains: an / domain (green) and a regulatory domain (blue). The catalytic triad residues are shown in ball-and-stick representations. (c) Nucleophile Ser157 in molecule A interact with -mercaptoethanol. The catalytic site consists of three residues: Ser157 (nucleophile), Glu251 (charge-relay network), and His281 (proton carrier). -mercaptoethanol is shown in ball-and-stick representations. A weighted electron density maps (2Fo - Fc) contoured at 1 in the vicinity of catalytic residues and -mercaptoethanol. (d) Substrate-binding tunnel. This tunnel of the hydrophobic pocket has an ovoidal shape with approximate depth of 16 Å. The nucleophile Ser157 residue is shown in ball-and-stick representations in the area of the orange dotted circle.

The above figure is reprinted by permission from John Wiley & Sons, Inc.: Proteins (2009, 74, 1036-1040) copyright 2009.