2C7B

The Crystal Structure of EstE1, a New Thermophilic and Thermostable Carboxylesterase Cloned from a Metagenomic Library

PDB DOI: https://doi.org/10.2210/pdb2C7B/pdb

Classification: HYDROLASE
Organism(s): uncultured archaeon
Expression System: Escherichia coli BL21(DE3)
Mutation(s): No

Deposited: 2005-11-21 Released: 2005-12-01
Deposition Author(s): Byun, J.-S., Rhee, J.-K., Kim, D.-U., Oh, J.-W., Cho, H.-S.

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 2.30 Å
R-Value Free: 0.261
R-Value Work: 0.234
R-Value Observed: 0.234

wwPDB Validation 3D Report Full Report

This is version 1.2 of the entry. See complete history.

Literature

Crystal Structure of Hyperthermophilic Esterase Este1 and the Relationship between its Dimerization and Thermostability Properties.

Byun, J.-S., Rhee, J.-K., Kim, N.D., Yoon, J., Kim, D.-U., Koh, E., Oh, J.-W., Cho, H.-S.

(2007) BMC Struct Biol 7: 47

PubMed: 17625021 Search on PubMedSearch on PubMed Central
DOI: https://doi.org/10.1186/1472-6807-7-47
Primary Citation of Related Structures:
2C7B

PubMed Abstract:
EstE1 is a hyperthermophilic esterase belonging to the hormone-sensitive lipase family and was originally isolated by functional screening of a metagenomic library constructed from a thermal environmental sample. Dimers and oligomers may have been evolutionally selected in thermophiles because intersubunit interactions can confer thermostability on the proteins. The molecular mechanisms of thermostabilization of this extremely thermostable esterase are not well understood due to the lack of structural information.

Organizational Affiliation

Department of Biology, Yonsei University, 134 Shinchon-dong, Seodaemun-gu, Seoul, Korea. lovemilk99@yonsei.ac.kr

Macromolecule Content

Total Structure Weight: 68.12 kDa
Atom Count: 4,607
Modelled Residue Count: 586
Deposited Residue Count: 622
Unique protein chains: 1

Macromolecules

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
CARBOXYLESTERASE	A, B	311	uncultured archaeon	Mutation(s): 0 EC: 3.1.1.1
UniProt
Find proteins for Q5G935 (Uncultured archaeon) Explore Q5G935 Go to UniProtKB: Q5G935
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	Q5G935
Sequence Annotations Expand
Reference Sequence

Small Molecules

Modified Residues 1 Unique
ID	Chains	Type	Formula	2D Diagram	Parent
MSE Query on MSE	A, B	L-PEPTIDE LINKING	C₅ H₁₁ N O₂ Se		MET

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 2.30 Å
R-Value Free: 0.261
R-Value Work: 0.234
R-Value Observed: 0.234
Space Group: P 4₁ 2₁ 2

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 73.71	α = 90
b = 73.71	β = 90
c = 234.23	γ = 90

Software Package:

Software Name	Purpose
CNS	refinement
MOSFLM	data reduction
SCALEPACK	data scaling

Structure Validation

View Full Validation Report

Entry History

Deposition Data

Released Date: 2005-12-01

Deposition Author(s):

Revision History (Full details and data files)

Version 1.0: 2005-12-01
Type: Initial release
Version 1.1: 2011-05-08
Changes: Version format compliance
Version 1.2: 2011-07-13
Changes: Version format compliance

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM133198.