2XQR

Crystal structure of plant cell wall invertase in complex with a specific protein inhibitor

Summary for 2XQR

• Entry DOI: 10.2210/pdb2xqr/pdb
• Related: 1RJ1 1RJ4 2CJ4 2CJ5 2CJ6 2CJ7 2CJ8
• Descriptor: BETA-FRUCTOFURANOSIDASE, INSOLUBLE ISOENZYME CWINV1, INVERTASE INHIBITOR, alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[beta-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (9 entities in total)
• Functional Keywords: hydrolase-inhibitor complex, apoplast, cell wall, hydrolase, protein inhibitor, sugar metabolism, glycosidase, hydrolase/inhibitor
• Biological source: ARABIDOPSIS THALIANA (THALE CRESS); More
• Total number of polymer chains: 12
• Total formula weight: 475514.11

Authors

Hothorn, M.,Van den Ende, W.,Lammens, W.,Rybin, V.,Scheffzek, K. (deposition date: 2010-09-07, release date: 2010-10-06, Last modification date: 2024-11-20)

Primary citation

Hothorn, M.,Van Den Ende, W.,Lammens, W.,Rybin, V.,Scheffzek, K.
Structural Insights Into the Ph-Controlled Targeting of Plant Cell-Wall Invertase by a Specific Inhibitor Protein.
Proc.Natl.Acad.Sci.USA, 107:17427-, 2010

PubMed Abstract: Invertases are highly regulated enzymes with essential functions in carbohydrate partitioning, sugar signaling, and plant development. Here we present the 2.6 Å crystal structure of Arabidopsis cell-wall invertase 1 (INV1) in complex with a protein inhibitor (CIF, or cell-wall inhibitor of β-fructosidase) from tobacco. The structure identifies a small amino acid motif in CIF that directly targets the invertase active site. The activity of INV1 and its interaction with CIF are strictly pH-dependent with a maximum at about pH 4.5. At this pH, isothermal titration calorimetry reveals that CIF tightly binds its target with nanomolar affinity. CIF competes with sucrose (Suc) for the same binding site, suggesting that both the extracellular Suc concentration and the pH changes regulate association of the complex. A conserved glutamate residue in the complex interface was previously identified as an important quantitative trait locus affecting fruit quality, which implicates the invertase-inhibitor complex as a main regulator of carbon partitioning in plants. Comparison of the CIF/INV1 structure with the complex between the structurally CIF-related pectin methylesterase inhibitor (PMEI) and pectin methylesterase indicates a common targeting mechanism in PMEI and CIF. However, CIF and PMEI use distinct surface areas to selectively inhibit very different enzymatic scaffolds.

PubMed: 20858733
DOI: 10.1073/PNAS.1004481107

Experimental method

X-RAY DIFFRACTION (2.58 Å)