PDBsum entry: 1np2

Hydrolase

PDB-id

1np2

Contents

Description

Header details

Protein chains

Waters ×334

* Residue conservation analysis

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PDB id:

1np2

Name:

Hydrolase

Title:

Crystal structure of thermostable beta-glycosidase from thermophilic eubacterium thermus nonproteolyticus hg102

Structure:

Beta-glycosidase. Chain: a, b. Engineered: yes

Source:

Thermus nonproteolyticus. Organism_taxid: 116039. Strain: hg102. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

UniProt:

Chains A, B: Q9L794 (Q9L794_9DEIN)

Seq:

Struc:

Seq:

436 a.a.

Struc:

426 a.a.

Key:		PfamA domain
		Secondary structure			CATH domain

Enzyme class:

E.C.3.2.1.21 [IntEnz] [ExPASy] [KEGG] [BRENDA]

Reaction:

Hydrolysis of terminal, non-reducing beta-D-glucose residues with release of beta-D-glucose.

Resolution:

2.40Å

R-factor:

0.230

R-free:

0.272

Authors:

D.C.Liang,W.R.Chang,X.Q.Wang,X.Y.He

Key ref:

X.Wang et al. (2003). Structural basis for thermostability of beta-glycosidase from the thermophilic eubacterium Thermus nonproteolyticus HG102.. J Bacteriol, 185, 4248-4255. [PubMed id: 12837801] [DOI: 10.1128/JB.185.14.4248-4255.2003]

Date:

16-Jan-03

Release date:

15-Jul-03

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Key reference

DOI no: 10.1128/JB.185.14.4248-4255.2003 J Bacteriol 185:4248-4255 (2003)

PubMed id: 12837801

Structural basis for thermostability of beta-glycosidase from the thermophilic eubacterium Thermus nonproteolyticus HG102.

X.Wang, X.He, S.Yang, X.An, W.Chang, D.Liang.

ABSTRACT

The three-dimensional structure of a thermostable beta-glycosidase (Gly(Tn)) from the thermophilic eubacterium Thermus nonproteolyticus HG102 was determined at a resolution of 2.4 A. The core of the structure adopts the (betaalpha)(8) barrel fold. The sequence alignments and the positions of the two Glu residues in the active center indicate that Gly(Tn) belongs to the glycosyl hydrolases of retaining family 1. We have analyzed the structural features of Gly(Tn) related to the thermostability and compared its structure with those of other mesophilic glycosidases from plants, eubacteria, and hyperthermophilic enzymes from archaea. Several possible features contributing to the thermostability of Gly(Tn) were elucidated.

Literature references that cite this PDB file's key reference

PubMed id Reference

17357157 A.Ausili, B.Cobucci-Ponzano, B.Di Lauro, R.D'Avino, G.Perugino, E.Bertoli, A.Scirè, M.Rossi, F.Tanfani, and M.Moracci (2007).
A comparative infrared spectroscopic study of glycoside hydrolases from extremophilic archaea revealed different molecular mechanisms of adaptation to high temperatures.

Proteins, 67, 991.

17503162 M.León, P.Isorna, M.Menéndez, J.Sanz-Aparicio, and J.Polaina (2007).
Comparative study and mutational analysis of distinctive structural elements of hyperthermophilic enzymes.

Protein J, 26, 435-444.

17526788 R.Miyake, J.Kawamoto, Y.L.Wei, M.Kitagawa, I.Kato, T.Kurihara, and N.Esaki (2007).
Construction of a low-temperature protein expression system using a cold-adapted bacterium, Shewanella sp. strain Ac10, as the host.

Appl Environ Microbiol, 73, 4849-4856.

15455210 Z.Silva, S.Alarico, and M.S.da Costa (2005).
Trehalose biosynthesis in Thermus thermophilus RQ-1: biochemical properties of the trehalose-6-phosphate synthase and trehalose-6-phosphate phosphatase.

Extremophiles, 9, 29-36.

The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time.