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Hydrolase PDB-id
1wl7
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Protein chain
312 a.a. *
Metal ions
_CA
Waters ×240

* Residue conservation analysis
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PDB id: 1wl7
Name: Hydrolase
Title: Structure of the thermostable arabinanase

Structure:
Arabinanase-ts. Chain: a. Synonym: endo-1,5-alpha-l-arabinanase, arabinase-ts, rabinan endo-1,5-alpha-l-arabinosidase. Engineered: yes

Source:
Geobacillus thermodenitrificans. Organism_taxid: 33940. Strain: ts-3. Expressed in: bacillus subtilis. Expression_system_taxid: 1423.

UniProt:
Q93HT9 (Q93HT9_9BACI) Pfam  
Seq:
Struc:
Seq: 313 a.a.
Struc: 312 a.a.
Key:    PfamA domain
 Secondary structure  CATH domain

Resolution:
1.90Å

R-factor:
0.183

R-free:
0.225

Authors:
A.Yamaguchi,T.Tada,T.Nakaniwa,T.Kitatani

Key ref:
A.Yamaguchi et al. (2005). Structural basis for thermostability of endo-1,5-alpha-L-arabinanase from Bacillus thermodenitrificans TS-3.. J Biochem (Tokyo), 137, 587-592. [PubMed id: 15944411] [DOI: 10.1093/jb/mvi078]

Date:
21-Jun-04

Release date:
21-Jun-05
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    Key reference    
 
 
DOI no: 10.1093/jb/mvi078 J Biochem (Tokyo) 137:587-592 (2005)
PubMed id: 15944411  
 
 
Structural basis for thermostability of endo-1,5-alpha-L-arabinanase from Bacillus thermodenitrificans TS-3.
A.Yamaguchi, T.Tada, K.Wada, T.Nakaniwa, T.Kitatani, Y.Sogabe, M.Takao, T.Sakai, K.Nishimura.
 
  ABSTRACT  
 
The crystal structure of a thermostable endo-1,5-alpha-L-arabinanase, ABN-TS, from Bacillus thermodenitrificans TS-3 was determined at 1.9 A to an R-factor of 18.3% and an R-free-factor of 22.5%. The enzyme molecule has a five-bladed beta-propeller fold. The substrate-binding cleft formed across one face of the propeller is open on both sides to allow random binding of several sugar units in the polymeric substrate arabinan. The beta-propeller fold is stabilized through a ring closure. ABN-TS exhibits a new closure-mode involving residues in the N-terminal region: Phe7 to Gly21 exhibit hydrogen bonds and hydrophobic interactions with the first and last blades, and Phe4 links the second and third blades through a hydrogen bond and an aromatic stacking interaction, respectively. The role of the N-terminal region in the thermostability was confirmed with a mutant lacking 16 amino acid residues from the N-terminus of ABN-TS.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
19505290 A.Alhassid, A.Ben-David, O.Tabachnikov, D.Libster, E.Naveh, G.Zolotnitsky, Y.Shoham, and G.Shoham (2009).
Crystal structure of an inverting GH 43 1,5-alpha-L-arabinanase from Geobacillus stearothermophilus complexed with its substrate.
  Biochem J, 422, 73-82.  
19129163 W.Lammens, K.Le Roy, L.Schroeven, A.Van Laere, A.Rabijns, and W.Van den Ende (2009).
Structural insights into glycoside hydrolase family 32 and 68 enzymes: functional implications.
  J Exp Bot, 60, 727-740.  
18483735 D.W.Wong, V.J.Chan, and S.B.Batt (2008).
Cloning and characterization of a novel exo-alpha-1,5-L-arabinanase gene and the enzyme.
  Appl Microbiol Biotechnol, 79, 941-949.  
17139091 M.Verhaest, W.Lammens, K.Le Roy, B.De Coninck, C.J.De Ranter, A.Van Laere, W.Van den Ende, and A.Rabijns (2006).
X-ray diffraction structure of a cell-wall invertase from Arabidopsis thaliana.
  Acta Crystallogr D Biol Crystallogr, 62, 1555-1563.
PDB code: 2ac1
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.