PDBsum entry: 1sqj

Hydrolase

PDB-id: 1sqj

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PROCHECK

Protein chains

770 a.a. *

Waters ×63

* Residue conservation analysis

Tools

Clefts Calculation

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PDB id:

1sqj

Name:

Hydrolase

Title:

Crystal structure analysis of oligoxyloglucan reducing-end- specific cellobiohydrolase (oxg-rcbh)

Structure:

Oligoxyloglucan reducing-end-specific cellobiohydrolase. Chain: a, b. Synonym: oxg-rcbh. Engineered: yes

Source:

Geotrichum sp. M128. Organism_taxid: 203496. Expressed in: escherichia coli. Expression_system_taxid: 562.

UniProt:

Chains A, B: Q8J0D2 (Q8J0D2_9ASCO)

Seq:

Struc:

Seq:

Struc:

Seq:

Struc:

Seq:

812 a.a.

Struc:

770 a.a.

Key:	PfamB domain
Secondary structure	CATH domain

Resolution:

2.20Å

R-factor:

0.219

R-free:

0.251

Authors:

K.Yaoi,H.Kondo,N.Noro,M.Suzuki,S.Tsuda,Y.Mitsuishi

Key ref:

K.Yaoi et al. (2004). Tandem repeat of a seven-bladed beta-propeller domain in oligoxyloglucan reducing-end-specific cellobiohydrolase.. Structure, 12, 1209-1217. [PubMed id: 15242597] [DOI: 10.1016/j.str.2004.04.020]

Date:

19-Mar-04

Release date:

20-Jul-04

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Clefts

Surface

Key reference

DOI no: 10.1016/j.str.2004.04.020

Structure 12:1209-1217 (2004)

PubMed id: 15242597

Tandem repeat of a seven-bladed beta-propeller domain in oligoxyloglucan reducing-end-specific cellobiohydrolase.

K.Yaoi, H.Kondo, N.Noro, M.Suzuki, S.Tsuda, Y.Mitsuishi.

ABSTRACT

Oligoxyloglucan reducing-end-specific cellobiohydrolase (OXG-RCBH; EC 3.2.1.150) is an exoglucanase that recognizes the reducing end of oligoxyloglucan and releases two glucosyl residue segments from the main chain. The X-ray crystal structure of OXG-RCBH determined at 2.2 A resolution reveals a unique feature of this enzyme; OXG-RCBH consists of a tandem repeat of two similar domains, which are both folded into seven-bladed beta-propeller structures. The sequence alignment of the propeller blades, based on the structure, indicates that a weak repeat of the amino acid sequence occurred seven times to construct each domain. There is a cleft that can accommodate the substrate oligosaccharide between the two domains, which is a putative substrate binding subsite. Mutation of either Asp35 or Asp465, located in the putative catalytic center, to Asn resulted in a protein with no detectable catalytic activity, indicating the critical role of these amino acids in catalysis.

Selected figure(s)

Figure 6.
Figure 6. Surface Representation of OXG-RCBHIllustration of the molecular surface of OXG-RCBH produced using GRASP (Nicholls et al., 1991), colored according to the electrostatic potential. The middle image is viewed from the same orientation as Figure 1. The images to the left and right are viewed from approximately 90° from the middle.

The above figure is reprinted by permission from Cell Press: Structure (2004, 12, 1209-1217) copyright 2004.

Figure was selected by an automated process.