1zlp

Petal death protein PSR132 with cysteine-linked glutaraldehyde forming a thiohemiacetal adduct

spinqualitylabelsall models 1zlp, resolution 2.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1zlp is a 2 chain structure with sequence from Dianthus caryophyllus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GAQ, MG Gene: PSR132 (Dianthus caryophyllus) Resources: FirstGlance, OCA, RCSB, PDBsum Function [CPPM_DIACA] Catalyzes cleavage of the C(2)-C(3) bond in oxaloacetate and in (2R)-alkyl malate derivatives to form oxalate and acetate, and alkyl carboxylates and R-ketocarboxylates, respectively. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Expression of the PSR132 protein from Dianthus caryophyllus (carnation, clover pink) is induced in response to ethylene production associated with petal senescence, and thus the protein is named petal death protein (PDP). Recent work has established that despite the annotation of PDP in sequence databases as carboxyphosphoenolpyruvate mutase, the enzyme is actually a C-C bond cleaving lyase exhibiting a broad substrate profile. The crystal structure of PDP has been determined at 2.7 A resolution, revealing a dimer-of-dimers oligomeric association. Consistent with sequence homology, the overall alpha/beta barrel fold of PDP is the same as that of other isocitrate lyase/PEP mutase superfamily members, including a swapped eighth helix within a dimer. Moreover, Mg(2+) binds in the active site of PDP with a coordination pattern similar to that seen in other superfamily members. A compound, covalently bound to the catalytic residue, Cys144, was interpreted as a thiohemiacetal adduct resulting from the reaction of glutaraldehyde used to cross-link the crystals. The Cys144-carrying flexible loop that gates access to the active site is in the closed conformation. Models of bound substrates and comparison with the closed conformation of isocitrate lyase and 2-methylisocitrate lyase revealed the structural basis for the broad substrate profile of PDP. Crystal structure of the petal death protein from carnation flower.,Teplyakov A, Liu S, Lu Z, Howard A, Dunaway-Mariano D, Herzberg O Biochemistry. 2005 Dec 20;44(50):16377-84. PMID:16342930 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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