2cj5
From Proteopedia
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CRYSTAL STRUCTURE OF A CELL WALL INVERTASE INHIBITOR FROM TOBACCO (PH 5.0)
Overview
Plant acid invertases catalyse the breakdown of sucrose. Their activity is, tightly regulated through interaction with specific protein inhibitors., The complex between the cell-wall invertase inhibitor Nt-CIF and its, target enzyme is stable only at acidic pH, as found in the plant cell, wall. Since the pH in this compartment can be modulated between pH 4 and 6, in planta, the rapid dissociation of the inhibitor-enzyme complex at, neutral pH may represent a regulatory event. Here, it is analyzed whether, the inhibitory component undergoes structural rearrangements upon changes, in the pH environment. Six crystal forms grown at pH 4.6-9.5 and, diffracting up to 1.63 Angstrom indicate only small structural changes in, CIF. This suggests that complex dissociation at neutral pH is mediated, ... [(full description)]
About this Structure
2CJ5 is a [Single protein] structure of sequence from [Nicotiana tabacum] with ACT and SO4 as [ligands]. Full crystallographic information is available from [OCA].
Reference
Multiple crystal forms of the cell-wall invertase inhibitor from tobacco support high conformational rigidity over a broad pH range., Hothorn M, Scheffzek K, Acta Crystallogr D Biol Crystallogr. 2006 Jun;62(Pt 6):665-70. Epub 2006, May 12. PMID:16699194
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