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PDBsum entry 1aal
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protein ligands Protein-protein interface(s) links
Serine protease inhibitor PDB id
1aal

 

 

 

 

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Contents
Protein chains
58 a.a. *
Ligands
PO4
Waters ×126
* Residue conservation analysis
PDB id:
1aal
Name: Serine protease inhibitor
Title: Structural effects induced by mutagenesis affected by crystal packing factors: the structure of a 30-51 disulfide mutant of basic pancreatic trypsin inhibitor
Structure: Bovine pancreatic trypsin inhibitor. Chain: a, b. Engineered: yes
Source: Bos taurus. Cattle. Organism_taxid: 9913
Resolution:
1.60Å     R-factor:   0.179    
Authors: C.Eigenbrot,M.Randal,A.A.Kossiakoff
Key ref: C.Eigenbrot et al. (1992). Structural effects induced by mutagenesis affected by crystal packing factors: the structure of a 30-51 disulfide mutant of basic pancreatic trypsin inhibitor. Proteins, 14, 75-87. PubMed id: 1384034
Date:
09-Apr-92     Release date:   31-Oct-93    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P00974  (BPT1_BOVIN) -  Pancreatic trypsin inhibitor from Bos taurus
Seq:
Struc: 		100 a.a.
58 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 

 
Proteins 14:75-87 (1992)
PubMed id: 1384034  
 
 
Structural effects induced by mutagenesis affected by crystal packing factors: the structure of a 30-51 disulfide mutant of basic pancreatic trypsin inhibitor.
C.Eigenbrot, M.Randal, A.A.Kossiakoff.
 
  ABSTRACT  
 
The X-ray structure of the C30V/C51A disulfide mutant of basic pancreatic trypsin inhibitor (BPTI) has been analyzed at 1.6 A resolution. The mutant crystallizes in a cell having two molecules in the asymmetric unit. The packing environments of these two molecules are quite different, allowing for an assessment of which among the observed structural changes result from the mutation and which are produced by lattice packing considerations. The removal of the 30-51 disulfide bridge has little apparent affect on the B-factors of segments of adjacent polypeptide chain, although there are distinct differences in the structure compared to wild-type BPTI crystal structures. Both of the two C30V/C51A molecules show differences at the mutation site when compared to another 30-51 disulfide mutant, C30A/C51A, presumably due to the larger steric bulk of a valine versus an alanine at residue 30. A comparison of the two independent C30V/C51A molecules indicates that there are significant differences between them even at the site of mutation. The description of the specific structural differences of each molecule differs in detail and suggests different conclusions about the nature of structural perturbation near 30-51. In addition, when these two molecules are compared to two different wild-type structures, which had been determined from different space groups, a somewhat different pattern of changes is observed. These findings indicate that crystal packing can influence the observed perturbations in mutant structures.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
17623851 M.Andrec, D.A.Snyder, Z.Zhou, J.Young, G.T.Montelione, and R.M.Levy (2007).
A large data set comparison of protein structures determined by crystallography and NMR: statistical test for structural differences and the effect of crystal packing.
  Proteins, 69, 449-465.  
15852307 C.S.Rapp, and R.M.Pollack (2005).
Crystal packing effects on protein loops.
  Proteins, 60, 103-109.  
11320305 A.Addlagatta, S.Krzywda, H.Czapinska, J.Otlewski, and M.Jaskolski (2001).
Ultrahigh-resolution structure of a BPTI mutant.
  Acta Crystallogr D Biol Crystallogr, 57, 649-663.
PDB code: 1g6x
10450092 C.A.Schiffer, and W.F.van Gunsteren (1999).
Accessibility and order of water sites in and around proteins: A crystallographic time-averaging study.
  Proteins, 36, 501-511.  
9672038 S.W.Rick, J.W.Erickson, and S.K.Burt (1998).
Reaction path and free energy calculations of the transition between alternate conformations of HIV-1 protease.
  Proteins, 32, 7.  
  9377467 T.E.Creighton (1997).
Protein folding coupled to disulphide bond formation.
  Biol Chem, 378, 731-744.  
  7538845 B.A.Schulman, and P.S.Kim (1994).
Hydrogen exchange in BPTI variants that do not share a common disulfide bond.
  Protein Sci, 3, 2226-2232.  
7908437 C.Eigenbrot, T.Gonzalez, J.Mayeda, P.Carter, W.Werther, T.Hotaling, J.Fox, and J.Kessler (1994).
X-ray structures of fragments from binding and nonbinding versions of a humanized anti-CD18 antibody: structural indications of the key role of VH residues 59 to 65.
  Proteins, 18, 49-62.
PDB codes: 1fgv 2fgw
8171030 F.F.Davidson, P.C.Loewen, and H.G.Khorana (1994).
Structure and function in rhodopsin: replacement by alanine of cysteine residues 110 and 187, components of a conserved disulfide bond in rhodopsin, affects the light-activated metarhodopsin II state.
  Proc Natl Acad Sci U S A, 91, 4029-4033.  
  8061607 K.V.Kishan, J.P.Zeelen, M.E.Noble, T.V.Borchert, and R.K.Wierenga (1994).
Comparison of the structures and the crystal contacts of trypanosomal triosephosphate isomerase in four different crystal forms.
  Protein Sci, 3, 779-787.
PDB codes: 1tpe 1tpf
16100954 T.V.Borchert, R.Abagyan, K.V.Kishan, J.P.Zeelen, and R.K.Wierenga (1993).
The crystal structure of an engineered monomeric triosephosphate isomerase, monoTIM: the correct modelling of an eight-residue loop.
  Structure, 1, 205-213.
PDB code: 1tri
1368433 C.Eigenbrot, and A.A.Kossiakoff (1992).
Structural consequences of mutation.
  Curr Opin Biotechnol, 3, 333-337.  
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.

 

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