PDBsum entry 9pap

Hydrolase (sulfhydryl proteinase)

PDB id: 9pap

Contents

Protein chain

212 a.a. *

Ligands

MOH ×29

Waters ×195

* Residue conservation analysis

PDB id:

9pap

Name:

Hydrolase (sulfhydryl proteinase)

Title:

Structure of papain refined at 1.65 angstroms resolution

Structure:

Papain. Chain: a. Engineered: yes

Source:

Carica papaya. Papaya. Organism_taxid: 3649

Resolution:

1.65Å R-factor: 0.161

Authors:

I.G.Kamphuis,J.Drenth

Key ref:

I.G.Kamphuis et al. (1984). Structure of papain refined at 1.65 A resolution. J Mol Biol, 179, 233-256. PubMed id: 6502713 DOI: 10.1016/0022-2836(84)90467-4

Date:

31-Mar-86 Release date: 24-Oct-86

Supersedes:

8pap

Protein chain

P00784  (PAPA1_CARPA) -  Papain from Carica papaya

Seq: 345 a.a.

Struc: 212 a.a.*

* PDB and UniProt seqs differ at 4 residue positions (black crosses)

Enzyme reactions

• Enzyme class: E.C.3.4.22.2 - papain.
• Reaction: Hydrolysis of proteins with broad specificity for peptide bonds, with preference for a residue bearing a large hydrophobic sidechain at the P2 position. Does not accept Val at P1'.

DOI no: 10.1016/0022-2836(84)90467-4

J Mol Biol 179:233-256 (1984)

PubMed id: 6502713

Structure of papain refined at 1.65 A resolution.

I.G.Kamphuis, K.H.Kalk, M.B.Swarte, J.Drenth.

ABSTRACT

Papain is a sulfhydryl protease from the latex of the papaya fruit. Its molecules consist of one polypeptide chain with 212 amino acid residues. The chain is folded into two domains with the active site in a groove between the domains. We have refined the crystal structure of papain, in which the sulfhydryl group was oxidized, by a restrained least-squares procedure at 1.65 A to an R-factor of 16.1%. The estimated accuracy in the atomic co-ordinates is 0.1 A, except for disordered atoms. All phi/psi angles for non-glycine residues are found within the outer limit boundary of a Ramachandran plot and this provides another check on the quality of the model. In the alpha-helical parts of the structure, the C = O bonds are directed more away from the helix axis than in a classical alpha-helix, leading to somewhat longer hydrogen bonds, 2.98 A, compared to 2.89 A. The hydrogen-bonding parameters and conformational angles in the anti-parallel beta-sheet structure show a large diversity. Hydrogen bonds in the core of the sheet are generally shorter than those at the more twisted ends. The average value is 2.91 A. The hydrogen bond distance Ni+3-Oi in turns is relatively long and the geometry is far from linear. Hydrogen bond formation, therefore, is perhaps not an essential prerequisite for turn formation. Although the crystallization medium is 62% (w/w) methanol in water, only 29 out of 224 solvent molecules can be regarded with any certainty as methanol molecules. The water molecules play an important role in maintaining structural stability. This is specially true for internal water. Twenty-one water molecules are located in contact areas between adjacent papain molecules. It seems as if the enzyme is trapped in a grid of water molecules with only a limited number of direct interactions between the protein molecules. The residues in the active site cleft belong to the most static parts of the structure. In general, disorder in atomic positions increases when going from the interior of the protein molecule to its surface. This behavior was quantified and it was found that the point of minimum disorder is near the molecular centroid.

Selected figure(s)

Figure 6.
FIG. 6. Schematic picture of the papain active site. Hydrogen bonds are shown as broken lines. M is a methanol and 42 a water molecule. A second water molecule is between Gln19 and Trp177.

The above figure is reprinted by permission from Elsevier: J Mol Biol (1984, 179, 233-256) copyright 1984.

Figure was selected by an automated process.