1f0i
From Proteopedia
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| - | [[Image:1f0i.jpg|left|200px]] | + | [[Image:1f0i.jpg|left|200px]] |
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| - | '''THE FIRST CRYSTAL STRUCTURE OF A PHOSPHOLIPASE D''' | + | {{Structure |
| + | |PDB= 1f0i |SIZE=350|CAPTION= <scene name='initialview01'>1f0i</scene>, resolution 1.4Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=PO4:PHOSPHATE ION'>PO4</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Phospholipase_D Phospholipase D], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.4.4 3.1.4.4] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''THE FIRST CRYSTAL STRUCTURE OF A PHOSPHOLIPASE D''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1F0I is a [ | + | 1F0I is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_sp. Streptomyces sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F0I OCA]. |
==Reference== | ==Reference== | ||
| - | The first crystal structure of a phospholipase D., Leiros I, Secundo F, Zambonelli C, Servi S, Hough E, Structure. 2000 Jun 15;8(6):655-67. PMID:[http:// | + | The first crystal structure of a phospholipase D., Leiros I, Secundo F, Zambonelli C, Servi S, Hough E, Structure. 2000 Jun 15;8(6):655-67. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10873862 10873862] |
[[Category: Phospholipase D]] | [[Category: Phospholipase D]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: phospholipase d]] | [[Category: phospholipase d]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:02:43 2008'' |
Revision as of 09:02, 20 March 2008
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| , resolution 1.4Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Phospholipase D, with EC number 3.1.4.4 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
THE FIRST CRYSTAL STRUCTURE OF A PHOSPHOLIPASE D
Overview
BACKGROUND: The phospholipase D (PLD) superfamily includes enzymes that are involved in phospholipid metabolism, nucleases, toxins and virus envelope proteins of unknown function. PLD hydrolyzes the terminal phosphodiester bond of phospholipids to phosphatidic acid and a hydrophilic constituent. Phosphatidic acid is a compound that is heavily involved in signal transduction. PLD also catalyses a transphosphatidylation reaction in the presence of phosphatidylcholine and a short-chained primary or secondary alcohol. RESULTS: The first crystal structure of a 54 kDa PLD has been determined to 1.9 A resolution using the multiwavelength anomalous dispersion (MAD) method on a single WO(4) ion and refined to 1.4 A resolution. PLD from the bacterial source Streptomyces sp. strain PMF consists of a single polypeptide chain that is folded into two domains. An active site is located at the interface between these domains. The presented structure supports the proposed superfamily relationship with the published structure of the 16 kDa endonuclease from Salmonella typhimurium. CONCLUSIONS: The structure of PLD provides insight into the structure and mode of action of not only bacterial, plant and mammalian PLDs, but also of a variety of enzymes as diverse as cardiolipin synthases, phosphatidylserine synthases, toxins, endonucleases, as well as poxvirus envelope proteins having a so far unknown function. The common features of these enzymes are that they can bind to a phosphodiester moiety, and that most of these enzymes are active as bi-lobed monomers or dimers.
About this Structure
1F0I is a Single protein structure of sequence from Streptomyces sp.. Full crystallographic information is available from OCA.
Reference
The first crystal structure of a phospholipase D., Leiros I, Secundo F, Zambonelli C, Servi S, Hough E, Structure. 2000 Jun 15;8(6):655-67. PMID:10873862
Page seeded by OCA on Thu Mar 20 11:02:43 2008
