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| | {{STRUCTURE_1t0a| PDB=1t0a | SCENE= }} | | {{STRUCTURE_1t0a| PDB=1t0a | SCENE= }} |
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| - | '''Crystal Structure of 2C-Methyl-D-Erythritol-2,4-cyclodiphosphate Synthase from Shewanella Oneidensis'''
| + | ===Crystal Structure of 2C-Methyl-D-Erythritol-2,4-cyclodiphosphate Synthase from Shewanella Oneidensis=== |
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| - | ==Overview==
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| - | Isopentenyl pyrophosphate (IPP) is a universal building block for the ubiquitous isoprenoids that are essential to all organisms. The enzymes of the non-mevalonate pathway for IPP synthesis, which is unique to many pathogenic bacteria, have recently been explored as targets for antibiotic development. Several crystal structures of 2C-methyl-D-erythritol-2,4-cyclophosphate (MECDP) synthase, the fifth of seven enzymes involved in the non-mevalonate pathway for synthesis of IPP, have been reported; however, the composition of metal ions in the active site and the presence of a hydrophobic cavity along the non-crystallographic threefold symmetry axis has varied between the reported structures. Here, the structure of MEDCP from Shewanella oneidensis MR1 (SO3437) was determined to 1.6 A resolution in the absence of substrate. The presence of a zinc ion in the active-site cleft, tetrahedrally coordinated by two histidine side chains, an aspartic acid side chain and an ambiguous fourth ligand, was confirmed by zinc anomalous diffraction. Based on analysis of anomalous diffraction data and typical metal-to-ligand bond lengths, it was concluded that an octahedral sodium ion was 3.94 A from the zinc ion. A hydrophobic cavity was observed along the threefold non-crystallographic symmetry axis, filled by a well defined non-protein electron density that could be modeled as farnesyl pyrophosphate (FPP), a downstream product of IPP, suggesting a possible feedback mechanism for enzyme regulation. The high-resolution data clarified the FPP-binding mode compared with previously reported structures. Multiple sequence alignment indicated that the residues critical to the formation of the hydrophobic cavity and for coordinating the pyrophosphate group of FPP are present in the majority of MEDCP synthase enzymes, supporting the idea of a specialized biological function related to FPP binding in a subfamily of MEDCP synthase homologs.
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| | + | (as it appears on PubMed at http://www.pubmed.gov), where 15502301 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_15502301}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Mixed alpha beta]] | | [[Category: Mixed alpha beta]] |
| | [[Category: Synthase]] | | [[Category: Synthase]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:20:36 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 15:21:02 2008'' |
Revision as of 12:21, 28 July 2008
Template:STRUCTURE 1t0a
Crystal Structure of 2C-Methyl-D-Erythritol-2,4-cyclodiphosphate Synthase from Shewanella Oneidensis
Template:ABSTRACT PUBMED 15502301
About this Structure
1T0A is a Single protein structure of sequence from Bacteria. Full crystallographic information is available from OCA.
Reference
Structure of 2C-methyl-D-erythritol-2,4-cyclodiphosphate synthase from Shewanella oneidensis at 1.6 A: identification of farnesyl pyrophosphate trapped in a hydrophobic cavity., Ni S, Robinson H, Marsing GC, Bussiere DE, Kennedy MA, Acta Crystallogr D Biol Crystallogr. 2004 Nov;60(Pt 11):1949-57. Epub 2004, Oct 20. PMID:15502301
Page seeded by OCA on Mon Jul 28 15:21:02 2008
