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Hydrolase PDB-id
1wza
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Protein chain
488 a.a. *
Metal ions
_CA ×2
Waters ×551

* Residue conservation analysis
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PDB id: 1wza
Name: Hydrolase
Title: Crystal structure of alpha-amylase from h.Orenii

Structure:
Alpha-amylase a. Chain: a. Fragment: residues 28-515. Engineered: yes. Other_details: halophilic and thermophilic

Source:
Halothermothrix orenii. Organism_taxid: 31909. Gene: amya. Expressed in: escherichia coli. Expression_system_taxid: 562.

UniProt:
Q8GPL8 (Q8GPL8_9FIRM) Pfam  
Seq:
Struc:
Seq: 515 a.a.
Struc: 488 a.a.
Key:    PfamA domain
 Secondary structure  CATH domain

Resolution:
1.60Å

R-factor:
0.186

R-free:
0.209

Authors:
N.Sivakumar,K.Swaminathan,N.Li

Key ref:
N.Sivakumar et al. (2006). Crystal structure of AmyA lacks acidic surface and provide insights into protein stability at poly-extreme condition.. FEBS Lett, 580, 2646-2652. [PubMed id: 16647060] [DOI: 10.1016/j.febslet.2006.04.017]

Date:
03-Mar-05

Release date:
11-Apr-06

Related entries:
1gvi
thermus moltogenic amylase
1sma
maltogenic amylase
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    Key reference    
 
 
DOI no: 10.1016/j.febslet.2006.04.017 FEBS Lett 580:2646-2652 (2006)
PubMed id: 16647060  
 
 
Crystal structure of AmyA lacks acidic surface and provide insights into protein stability at poly-extreme condition.
N.Sivakumar, N.Li, J.W.Tang, B.K.Patel, K.Swaminathan.
 
  ABSTRACT  
 
Here we report the first crystal structure of a protein, AmyA, a secretory alpha-amylase isolated from Halothermothrix orenii, which is both halophilic and thermophilic. The crystal structure was determined at 1.6 A resolution. AmyA lacks the conserved acidic surface, which is considered essential for protein stability at high salinity. Sedimentation velocity and CD experiments on AmyA reveal the formation of unique reversible poly-dispersed oligomers that show unusually high thermal stability. These studies provide valuable insight into the structural elements that contribute to the stability of AmyA at both physical and chemical extremes and their functional implications.
 
  Selected figure(s)  
 
Figure 1.
 
  The above figure is reprinted by permission from the Federation of European Biochemical Societies: FEBS Lett (2006, 580, 2646-2652) copyright 2006.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
19698123 J.A.Winter, P.Christofi, S.Morroll, and K.A.Bunting (2009).
The crystal structure of Haloferax volcanii proliferating cell nuclear antigen reveals unique surface charge characteristics due to halophilic adaptation.
  BMC Struct Biol, 9, 55.  
19145256 K.Mavromatis, N.Ivanova, I.Anderson, A.Lykidis, S.D.Hooper, H.Sun, V.Kunin, A.Lapidus, P.Hugenholtz, B.Patel, and N.C.Kyrpides (2009).
Genome analysis of the anaerobic thermohalophilic bacterium Halothermothrix orenii.
  PLoS ONE, 4, e4192.  
17310272 S.Srimathi, G.Jayaraman, G.Feller, B.Danielsson, and P.R.Narayanan (2007).
Intrinsic halotolerance of the psychrophilic alpha-amylase from Pseudoalteromonas haloplanktis.
  Extremophiles, 11, 505-515.  
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.