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PDBsum entry 1ir7
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Hydrolase PDB id
1ir7

 

 

 

 

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Contents
Protein chain
129 a.a. *
Waters ×63
* Residue conservation analysis
PDB id:
1ir7
Name: Hydrolase
Title: Im mutant of lysozyme
Structure: Lysozyme. Chain: a. Synonym: lysozymE C. Engineered: yes. Mutation: yes
Source: Gallus gallus. Chicken. Organism_taxid: 9031. Tissue: egg white. Expressed in: saccharomyces cerevisiae. Expression_system_taxid: 4932.
Resolution:
1.90Å     R-factor:   0.174    
Authors: T.Ohmura,T.Ueda,Y.Hashimoto,T.Imoto
Key ref: T.Ohmura et al. (2001). Tolerance of point substitution of methionine for isoleucine in hen egg white lysozyme. Protein Eng, 14, 421-425. PubMed id: 11477222
Date:
19-Sep-01     Release date:   03-Oct-01    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P00698  (LYSC_CHICK) -  Lysozyme C from Gallus gallus
Seq:
Struc: 		147 a.a.
129 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.3.2.1.17  - lysozyme.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Hydrolysis of the 1,4-beta-linkages between N-acetyl-D-glucosamine and N-acetylmuramic acid in peptidoglycan heteropolymers of the prokaryotes cell walls.

 

 
Protein Eng 14:421-425 (2001)
PubMed id: 11477222  
 
 
Tolerance of point substitution of methionine for isoleucine in hen egg white lysozyme.
T.Ohmura, T.Ueda, Y.Hashimoto, T.Imoto.
 
  ABSTRACT  
 
X-ray structure determination of proteins by using the multiple-wavelength anomalous dispersion method targeting selenomethionine is now widely employed. Isoleucine was examined for the second choice of the substitution of methionine next to leucine. We performed a systematic mutational study of the substitutions of methionine for isoleucine. All mutated lysozymes were less stable than the wild-type by about 1 kcal/mol and it is suggested that this instability was caused by the change in residual hydrophobicity from isoleucine to methionine. The X-ray structures of all mutant lysozymes were very similar to that of the wild-type. In addition, both the accessible surface areas and the conformation of the side chain of methionine in all mutant lysozymes were similar to those of the side chain at the respective isoleucine in the wild-type. Therefore, it is suggested that the mutation from isoleucine to methionine in a protein can be considered as a "safe" substitution.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21283701 Z.Liu, F.Fan, X.Xiao, and Y.Sun (2011).
Constitutive Activation of the Thyroid-Stimulating Hormone Receptor (TSHR) by Mutating Ile in the Cytoplasmic Tail Segment.
  PLoS One, 6, e16335.  
20818390 D.Sun, G.Lee, J.H.Lee, H.Y.Kim, H.W.Rhee, S.Y.Park, K.J.Kim, Y.Kim, B.Y.Kim, J.I.Hong, C.Park, H.E.Choy, J.H.Kim, Y.H.Jeon, and J.Chung (2010).
A metazoan ortholog of SpoT hydrolyzes ppGpp and functions in starvation responses.
  Nat Struct Mol Biol, 17, 1188-1194.
PDB codes: 3nqw 3nr1
19217866 A.P.Yamniuk, H.Ishida, D.Lippert, and H.J.Vogel (2009).
Thermodynamic effects of noncoded and coded methionine substitutions in calmodulin.
  Biophys J, 96, 1495-1507.  
  18931446 M.Senda, S.Muto, M.Horikoshi, and T.Senda (2008).
Effect of leucine-to-methionine substitutions on the diffraction quality of histone chaperone SET/TAF-Ibeta/INHAT crystals.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 64, 960-965.  
17668378 E.P.Kirk, M.Sunde, M.W.Costa, S.A.Rankin, O.Wolstein, M.L.Castro, T.L.Butler, C.Hyun, G.Guo, R.Otway, J.P.Mackay, L.B.Waddell, A.D.Cole, C.Hayward, A.Keogh, P.Macdonald, L.Griffiths, D.Fatkin, G.F.Sholler, A.M.Zorn, M.P.Feneley, D.S.Winlaw, and R.P.Harvey (2007).
Mutations in cardiac T-box factor gene TBX20 are associated with diverse cardiac pathologies, including defects of septation and valvulogenesis and cardiomyopathy.
  Am J Hum Genet, 81, 280-291.  
16444766 D.M.Lehman, J.Hamlington, K.J.Hunt, R.J.Leach, R.Arya, H.Abboud, R.Duggirala, J.Blangero, H.H.Göring, and M.P.Stern (2006).
A novel missense mutation in ADRB3 increases risk for type 2 diabetes in a Mexican American family.
  Diabetes Metab Res Rev, 22, 331-336.  
16221305 P.Walasek, and J.F.Honek (2005).
Nonnatural amino acid incorporation into the methionine 214 position of the metzincin Pseudomonas aeruginosa alkaline protease.
  BMC Biochem, 6, 21.  
12021450 S.C.Kwok, C.T.Mant, and R.S.Hodges (2002).
Importance of secondary structural specificity determinants in protein folding: insertion of a native beta-sheet sequence into an alpha-helical coiled-coil.
  Protein Sci, 11, 1519-1531.  
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 codes are shown on the right.

 

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