PDBsum entry 2ci2

Proteinase inhibitor (chymotrypsin)

PDB id

2ci2

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Contents

			Protein chain

					65 a.a. *

			Waters ×64

* Residue conservation analysis

PDB id:

2ci2

Links

Name:

Proteinase inhibitor (chymotrypsin)

Title:

Crystal and molecular structure of the serine proteinase inhibitor ci- 2 from barley seeds

Structure:

Chymotrypsin inhibitor 2. Chain: i. Engineered: yes

Source:

Hordeum vulgare. Organism_taxid: 4513

Biol. unit:

Hexamer (from PQS)

Resolution:

2.00Å

R-factor:

0.198

Authors:

C.A.Mcphalen,M.N.G.James

Key ref:

C.A.McPhalen and M.N.James (1987). Crystal and molecular structure of the serine proteinase inhibitor CI-2 from barley seeds. Biochemistry, 26, 261-269. PubMed id: 3828302 DOI: 10.1021/bi00375a036

Date:

05-Sep-88

Release date:

07-Sep-88

Supersedes:

1ci2

PROCHECK

	Headers

	References

Protein chain

P01053 (ICI2_HORVU) - Subtilisin-chymotrypsin inhibitor-2A from Hordeum vulgare

Seq: Struc:					84 a.a. 65 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.?

[IntEnz] [ExPASy] [KEGG] [BRENDA]

DOI no: 10.1021/bi00375a036	Biochemistry 26:261-269 (1987)
PubMed id: 3828302

Crystal and molecular structure of the serine proteinase inhibitor CI-2 from barley seeds.
C.A.McPhalen, M.N.James.

ABSTRACT

Chymotrypsin inhibitor 2 (CI-2), a serine proteinase inhibitor from barley seeds, has been crystallized and its three-dimensional structure determined at 2.0-A resolution by the molecular replacement method. The structure has been refined by restrained-parameter least-squares methods to a crystallographic R factor (= sigma parallel Fo magnitude of-Fo parallel/sigma magnitude of Fo) o of 0.198. CI-2 is a member of the potato inhibitor 1 family. It lacks the characteristic stabilizing disulfide bonds of most other members of serine proteinase inhibitor families. The body of CI-2 shows few conformational changes between the free inhibitor and the previously reported structure of CI-2 in complex with subtilisin Novo [McPhalen, C.A., Svendsen, I., Jonassen, I., & James, M.N.G. (1985) Proc. Natl. Acad. Sci. U.S.A. 82, 7242-7246]. However, the reactive site loop has some significant conformational differences between the free inhibitor and its complexed form. The residues in this segment of polypeptide exhibit relatively large thermal motion parameters and some disorder in the uncomplexed form of the inhibitor. The reactive site bond is between Met-59I and Glu-60I in the consecutive sequential numbering of CI-2 (Met-60-Glu-61 according to the alignment of Svendsen et al. [Svendsen, I., Hejgaard, J., & Chavan, J.K. (1984) Carlsberg Res. Commun. 49, 493-502]). The network of hydrogen bonds and electrostatic interactions stabilizing the conformation of the reactive site loop is much less extensive in the free than in the complexed inhibitor.

Literature references that cite this PDB file's key reference

PubMed id

Reference

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PDB code:

1pju

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Single-molecule protein folding: diffusion fluorescence resonance energy transfer studies of the denaturation of chymotrypsin inhibitor 2.

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10737939

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10328267

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PDB code:

2wbc

10591104

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Proc Natl Acad Sci U S A, 96, 1257-1261.

PDB code:

1cq4

9609709

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PDB code:

1mit

8823186

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PDB code:

1eai

8278384

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Direct observation of better hydration at the N terminus of an alpha-helix with glycine rather than alanine as the N-cap residue.

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PDB codes:

1ypa 1ypb 1ypc

8497488

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PDB code:

1egl

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Use of restrained molecular dynamics in water to determine three-dimensional protein structure: prediction of the three-dimensional structure of Ecballium elaterium trypsin inhibitor II.

Proteins, 6, 405-417.

PDB code:

2eti

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