1ah7: Difference between revisions

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New page: left|200px<br /> <applet load="1ah7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ah7, resolution 1.501Å" /> '''PHOSPHOLIPASE C FR...
 
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==About this Structure==
==About this Structure==
1AH7 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Bacillus_cereus Bacillus cereus]] with ZN as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.4.3 3.1.4.3]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AH7 OCA]].  
1AH7 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Bacillus_cereus Bacillus cereus]] with ZN as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/Phospholipase_C Phospholipase C]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.4.3 3.1.4.3]]. Structure known Active Sites: CAT, ZNA, ZNB and ZNC. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AH7 OCA]].  


==Reference==
==Reference==
High-resolution (1.5 A) crystal structure of phospholipase C from Bacillus cereus., Hough E, Hansen LK, Birknes B, Jynge K, Hansen S, Hordvik A, Little C, Dodson E, Derewenda Z, Nature. 1989 Mar 23;338(6213):357-60. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=2493587 2493587]
High-resolution (1.5 A) crystal structure of phospholipase C from Bacillus cereus., Hough E, Hansen LK, Birknes B, Jynge K, Hansen S, Hordvik A, Little C, Dodson E, Derewenda Z, Nature. 1989 Mar 23;338(6213):357-60. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=2493587 2493587]
[[Category: Bacillus cereus]]
[[Category: Bacillus cereus]]
[[Category: Phospholipase C]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Greaves, R.]]
[[Category: Greaves, R.]]
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[[Category: phospholipid hydrolysis]]
[[Category: phospholipid hydrolysis]]


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Revision as of 13:29, 30 October 2007

File:1ah7.gif


1ah7, resolution 1.501Å

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PHOSPHOLIPASE C FROM BACILLUS CEREUS

OverviewOverview

Both the phosphatidylinositol-hydrolysing and the, phosphatidylcholine-hydrolysing phospholipases C have been implicated in, the generation of second messengers in mammalian cells. The, phosphatidylcholine-hydrolysing phospholipase C (PLC) from Bacillus, cereus, a monomeric protein containing 245 amino-acid residues, is similar, to some of the corresponding mammalian proteins. This, together with the, fact that the bacterial enzyme can mimic the action of mammalian PLC in, causing, for example, enhanced prostaglandin biosynthesis, suggests that, B. cereus PLC can be used as a model for the hitherto poorly characterized, mammalian PLCs. We report here the three-dimensional structure of B., cereus PLC at 1.5 A resolution. The enzyme is an all-helix protein, belonging to a novel structural ... [(full description)]

About this StructureAbout this Structure

1AH7 is a [Single protein] structure of sequence from [Bacillus cereus] with ZN as [ligand]. Active as [Phospholipase C], with EC number [3.1.4.3]. Structure known Active Sites: CAT, ZNA, ZNB and ZNC. Full crystallographic information is available from [OCA].

ReferenceReference

High-resolution (1.5 A) crystal structure of phospholipase C from Bacillus cereus., Hough E, Hansen LK, Birknes B, Jynge K, Hansen S, Hordvik A, Little C, Dodson E, Derewenda Z, Nature. 1989 Mar 23;338(6213):357-60. PMID:2493587

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