1zlp: Difference between revisions
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|PDB= 1zlp |SIZE=350|CAPTION= <scene name='initialview01'>1zlp</scene>, resolution 2.70Å | |PDB= 1zlp |SIZE=350|CAPTION= <scene name='initialview01'>1zlp</scene>, resolution 2.70Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=GAQ:5-HYDROXYPENTANAL'>GAQ</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= PSR132 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3570 Dianthus caryophyllus]) | |GENE= PSR132 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3570 Dianthus caryophyllus]) | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1zlp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zlp OCA], [http://www.ebi.ac.uk/pdbsum/1zlp PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1zlp RCSB]</span> | |||
}} | }} | ||
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[[Category: Lu, Z.]] | [[Category: Lu, Z.]] | ||
[[Category: Teplyakov, A.]] | [[Category: Teplyakov, A.]] | ||
[[Category: 2-propyl-3-methylmalate lyase]] | [[Category: 2-propyl-3-methylmalate lyase]] | ||
[[Category: helix swapping]] | [[Category: helix swapping,2-ethyl-3-methylmalate lyase]] | ||
[[Category: lyase/pep mutase superfamily]] | [[Category: lyase/pep mutase superfamily]] | ||
[[Category: tim-barrel]] | [[Category: tim-barrel]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:38:22 2008'' | ||
Revision as of 01:38, 31 March 2008
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| , resolution 2.70Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | PSR132 (Dianthus caryophyllus) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Petal death protein PSR132 with cysteine-linked glutaraldehyde forming a thiohemiacetal adduct
OverviewOverview
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.
About this StructureAbout this Structure
1ZLP is a Single protein structure of sequence from Dianthus caryophyllus. Full crystallographic information is available from OCA.
ReferenceReference
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
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