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| - | [[Image:1e5m.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1e5m| PDB=1e5m | SCENE= }} | | {{STRUCTURE_1e5m| PDB=1e5m | SCENE= }} |
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| - | '''BETA KETOACYL ACYL CARRIER PROTEIN SYNTHASE II (KASII) FROM SYNECHOCYSTIS SP.'''
| + | ===BETA KETOACYL ACYL CARRIER PROTEIN SYNTHASE II (KASII) FROM SYNECHOCYSTIS SP.=== |
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| - | ==Overview==
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| - | Condensing enzymes, catalyzing the formation of carbon-carbon bonds in several biosynthetic pathways, have lately been recognized as potential drug targets against cancer and tuberculosis, as crucial for combinatorial biosynthesis of antibiotics and related compounds, and as determinants of plant oil composition. beta-Ketoacyl-ACP synthases (KAS) are the condensing enzymes present in the fatty acid biosynthesis pathway and are able to elongate an acyl chain bound to either co-enzyme A (CoA) or acyl carrier protein (ACP) with a two-carbon unit derived from malonyl-ACP. Several isoforms of KAS with different substrate specificity are present in most species. We have determined the crystal structure of KAS II from Synechocystis sp. PCC 6803 to 1.54 A resolution giving a detailed description of the active site geometry. In order to analyze the structure-function relationships in this class of enzymes in more detail, we have compared all presently known three-dimensional structures of condensing enzymes from different pathways. The comparison reveals that these enzymes can be divided into three structural and functional classes. This classification can be related to variations in the catalytic mechanism and the set of residues in the catalytic site, e.g. due to differences in the nature of the second substrate providing the two-carbon elongation unit. The variation in the acyl-carrier (ACP or CoA) specificity might also be connected to this classification and residues involved in ACP binding in structure class 2 can be suggested based on the comparison. Finally, the two subunits in the dimer contribute differently to formation of the substrate binding-pocket in the three structural classes.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_11152607}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 11152607 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_11152607}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Carbon-carbon bond formation]] | | [[Category: Carbon-carbon bond formation]] |
| | [[Category: Condensing enzyme]] | | [[Category: Condensing enzyme]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:41:38 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 00:11:12 2008'' |
Revision as of 21:11, 30 June 2008
Template:STRUCTURE 1e5m
BETA KETOACYL ACYL CARRIER PROTEIN SYNTHASE II (KASII) FROM SYNECHOCYSTIS SP.
Template:ABSTRACT PUBMED 11152607
About this Structure
1E5M is a Single protein structure of sequence from Synechocystis sp.. Full crystallographic information is available from OCA.
Reference
The crystal structure of beta-ketoacyl-acyl carrier protein synthase II from Synechocystis sp. at 1.54 A resolution and its relationship to other condensing enzymes., Moche M, Dehesh K, Edwards P, Lindqvist Y, J Mol Biol. 2001 Jan 19;305(3):491-503. PMID:11152607
Page seeded by OCA on Tue Jul 1 00:11:12 2008
