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PDBsum entry 1pyt

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Ternary complex (zymogen) PDB id
1pyt
Contents
Protein chains
94 a.a. *
309 a.a. *
248 a.a. *
251 a.a. *
Metals
_ZN
_CA
Waters ×381
* Residue conservation analysis

References listed in PDB file
Key reference
Title The three-Dimensional structure of the native ternary complex of bovine pancreatic procarboxypeptidase a with proproteinase e and chymotrypsinogen c.
Authors F.X.Gomis-Rüth, M.Gómez, W.Bode, R.Huber, F.X.Avilés.
Ref. Embo J, 1995, 14, 4387-4394.
PubMed id 7556081
Abstract
The metalloexozymogen procarboxypeptidase A is mainly secreted in ruminants as a ternary complex with zymogens of two serine endoproteinases, chymotrypsinogen C and proproteinase E. The bovine complex has been crystallized, and its molecular structure analysed and refined at 2.6 A resolution to an R factor of 0.198. In this heterotrimer, the activation segment of procarboxypeptidase A essentially clamps the other two subunits, which shield the activation sites of the former from tryptic attack. In contrast, the propeptides of both serine proproteinases are freely accessible to trypsin. This arrangement explains the sequential and delayed activation of the constituent zymogens. Procarboxypeptidase A is virtually identical to the homologous monomeric porcine form. Chymotrypsinogen C displays structural features characteristic for chymotrypsins as well as elastases, except for its activation domain; similar to bovine chymotrypsinogen A, its binding site is not properly formed, while its surface located activation segment is disordered. The proproteinase E structure is fully ordered and strikingly similar to active porcine elastase; its specificity pocket is occluded, while the activation segment is fixed to the molecular surface. This first structure of a native zymogen from the proteinase E/elastase family does not fundamentally differ from the serine proproteinases known so far.
Added reference #1*
Title Determination of hemihedral twinning and initial structural analysis of crystals of the procarboxypeptidase A ternary complex.
Authors F.X.Gomis-Rüth, I.Fita, R.Kiefersauer, R.Huber, F.X.Avilés, J.Navaza.
Ref. Acta Crystallogr D Biol Crystallogr, 1995, 51, 819-823. [DOI no: 10.1107/S0907444995000643]
PubMed id 15299814
Full text Abstract
Figure 1.
Fig. 1. (a) Graphical representation for different twinning fractions a of he theretical cumulative distribution funtion (Z, ot), where Z epresents the intensity relative to the mean intesity, giving the fraction of eflections having an intensity less than Z. This function, for non­centrosymmetric reflections of crystals, is given by (3 and 4) in the text. Note that N(Z, ct) = N[Z, (I ­ a]. (b) Experimental N(Z) curves. A comparison with the theoretical distribution for ot = 0.0 (thickest, solid line) as a reference is included. Six untwinned data sets arbitrarily chosen (R. Huber, unpublihed results; hin lines) display an exponential habitus and are always located bove the theoretical distribution for an untwinned crystal. TC data (thick, soli line), so as a further data set (R. Huber, unpublished results; thick dashed line) for which twinning was suspected, render a sigmoid habitus and lie below the theoretical values.
The above figure is reproduced from the cited reference with permission from the IUCr
*Note, "added" references are those not in the PDB file but which have either been obtained from the journal or suggested by the author(s).
Secondary reference #1
Title Procarboxypeptidase a-S6 : detailed structure analysis of the constituting subunits and implications for their activation
Authors F.X.Gomis-Ruth, M.Gomez, J.Vendrell, S.Ventura, W.Bode, R.Huber, F.X.Aviles.
Ref. TO BE PUBLISHED ...
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