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PDBsum entry 1mua

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Lyase(oxo-acid) PDB id
1mua
Jmol
Contents
Protein chain
256 a.a.
Metals
_HG
_ZN
Waters ×91

References listed in PDB file
Key reference
Title Structure and energetics of a non-Proline cis-Peptidyl linkage in a proline-202-->Alanine carbonic anhydrase ii variant.
Authors N.B.Tweedy, S.K.Nair, S.A.Paterno, C.A.Fierke, D.W.Christianson.
Ref. Biochemistry, 1993, 32, 10944-10949. [DOI no: 10.1021/bi00092a003]
PubMed id 8218160
Note: In the PDB file this reference is annotated as "TO BE PUBLISHED". The citation details given above were obtained from the PDBe's Unpublished References server.
Abstract
The crystal structure of a human carbonic anhydrase II (CAII) variant, cis-proline-202-->alanine (P202A), has been determined at 1.7-A resolution, indicating that the wild-type geometry, including the cis-peptidyl linkage, is retained upon substitution of proline by alanine. The CO2 hydrase activity and affinity for sulfonamide inhibitors of P202A CAII are virtually identical to those of wild type. However, the substitution of cis-alanine for cis-proline decreases the stability of the folded state by approximately 5 kcal mol-1 relative to both the unfolded state and an equilibrium intermediate in guanidine hydrochloride-induced denaturation. This destabilization can be attributed mainly to the less favorable cis/trans equilibrium of Xaa-alanine bonds compared to Xaa-proline bonds in the denatured state although other factors, including increased conformational entropy of the denatured state and decreased packing interactions in the native state, also contribute to the observed destabilization. The high catalytic activity of P202A CAII illustrates that unfavorable local conformations are nonetheless endured to satisfy the precise structural requirements of catalysis and ligand binding in the CAII active site.
PROCHECK
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