1f0i

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[[Image:1f0i.jpg|left|200px]]
[[Image:1f0i.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 1f0i |SIZE=350|CAPTION= <scene name='initialview01'>1f0i</scene>, resolution 1.4&Aring;
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The line below this paragraph, containing "STRUCTURE_1f0i", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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|GENE=
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|DOMAIN=
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{{STRUCTURE_1f0i| PDB=1f0i | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1f0i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f0i OCA], [http://www.ebi.ac.uk/pdbsum/1f0i PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1f0i RCSB]</span>
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'''THE FIRST CRYSTAL STRUCTURE OF A PHOSPHOLIPASE D'''
'''THE FIRST CRYSTAL STRUCTURE OF A PHOSPHOLIPASE D'''
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[[Category: Servi, S.]]
[[Category: Servi, S.]]
[[Category: Zambonelli, C.]]
[[Category: Zambonelli, C.]]
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[[Category: alpha-beta-alpha-beta-alpha structure]]
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[[Category: Alpha-beta-alpha-beta-alpha structure]]
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[[Category: phospholipase d]]
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[[Category: Phospholipase d]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:44:46 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:13:19 2008''
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Revision as of 12:44, 2 May 2008

Template:STRUCTURE 1f0i

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 Fri May 2 15:44:46 2008

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