spacer
spacer
Go to PDB code: 
protein Protein-protein interface(s) links
Hydrolase PDB id
1sqj
Jmol
Contents
Protein chains
770 a.a. *
Waters ×63
* Residue conservation analysis
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.
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    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam  
Q8J0D2  (CBHRE_GEOS1) -  Oligoxyloglucan reducing end-specific cellobiohydrolase
Seq:
Struc: 		 
Seq:
Struc: 		812 a.a.
770 a.a.
Key:    Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.3.2.1.150  - Oligoxyloglucan reducing-end-specific cellobiohydrolase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     metabolic process   4 terms 
  Biochemical function     hydrolase activity     3 terms  

 

 
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.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
19594936 E.M.Quistgaard, and S.S.Thirup (2009).
Sequence and structural analysis of the Asp-box motif and Asp-box beta-propellers; a widespread propeller-type characteristic of the Vps10 domain family and several glycoside hydrolase families.
  BMC Struct Biol, 9, 46.  
19682300 K.Yaoi, H.Kondo, A.Hiyoshi, N.Noro, H.Sugimoto, S.Tsuda, and K.Miyazaki (2009).
The crystal structure of a xyloglucan-specific endo-beta-1,4-glucanase from Geotrichum sp. M128 xyloglucanase reveals a key amino acid residue for substrate specificity.
  FEBS J, 276, 5094-5100.
PDB code: 3a0f
17680689 T.J.Stevens, and M.Paoli (2008).
RCC1-like repeat proteins: a pangenomic, structurally diverse new superfamily of beta-propeller domains.
  Proteins, 70, 378-387.  
17005254 C.D.Krause, Z.H.Yang, Y.S.Kim, J.H.Lee, J.R.Cook, and S.Pestka (2007).
Protein arginine methyltransferases: evolution and assessment of their pharmacological and therapeutic potential.
  Pharmacol Ther, 113, 50-87.  
17229143 T.Desmet, T.Cantaert, P.Gualfetti, W.Nerinckx, L.Gross, C.Mitchinson, and K.Piens (2007).
An investigation of the substrate specificity of the xyloglucanase Cel74A from Hypocrea jecorina.
  FEBS J, 274, 356-363.  
17922847 T.Ishida, K.Yaoi, A.Hiyoshi, K.Igarashi, and M.Samejima (2007).
Substrate recognition by glycoside hydrolase family 74 xyloglucanase from the basidiomycete Phanerochaete chrysosporium.
  FEBS J, 274, 5727-5736.  
17376777 T.M.Gloster, F.M.Ibatullin, K.Macauley, J.M.Eklöf, S.Roberts, J.P.Turkenburg, M.E.Bjørnvad, P.L.Jørgensen, S.Danielsen, K.S.Johansen, T.V.Borchert, K.S.Wilson, H.Brumer, and G.J.Davies (2007).
Characterization and three-dimensional structures of two distinct bacterial xyloglucanases from families GH5 and GH12.
  J Biol Chem, 282, 19177-19189.
PDB codes: 2jem 2jen 2jep 2jeq
16772298 C.Martinez-Fleites, C.I.Guerreiro, M.J.Baumann, E.J.Taylor, J.A.Prates, L.M.Ferreira, C.M.Fontes, H.Brumer, and G.J.Davies (2006).
Crystal structures of Clostridium thermocellum xyloglucanase, XGH74A, reveal the structural basis for xyloglucan recognition and degradation.
  J Biol Chem, 281, 24922-24933.
PDB codes: 2cn2 2cn3
16332739 K.Yaoi, T.Nakai, Y.Kameda, A.Hiyoshi, and Y.Mitsuishi (2005).
Cloning and characterization of two xyloglucanases from Paenibacillus sp. strain KM21.
  Appl Environ Microbiol, 71, 7670-7678.  
15718242 S.Fushinobu, M.Hidaka, Y.Honda, T.Wakagi, H.Shoun, and M.Kitaoka (2005).
Structural basis for the specificity of the reducing end xylose-releasing exo-oligoxylanase from Bacillus halodurans C-125.
  J Biol Chem, 280, 17180-17186.
PDB codes: 1wu4 1wu5 1wu6
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. Where a reference describes a PDB structure, the PDB code is shown on the right.