From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:2o1s.jpg|left|200px]] | + | {{Seed}} |
| | + | [[Image:2o1s.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_2o1s| PDB=2o1s | SCENE= }} | | {{STRUCTURE_2o1s| PDB=2o1s | SCENE= }} |
| | | | |
| - | '''1-deoxy-D-xylulose 5-phosphate synthase (DXS) from Escherichia coli'''
| + | ===1-deoxy-D-xylulose 5-phosphate synthase (DXS) from Escherichia coli=== |
| | | | |
| | | | |
| - | ==Overview==
| + | <!-- |
| - | Isopentenyl pyrophosphate (IPP) is a common precursor for the synthesis of all isoprenoids, which have important functions in living organisms. IPP is produced by the mevalonate pathway in archaea, fungi, and animals. In contrast, IPP is synthesized by a mevalonate-independent pathway in most bacteria, algae, and plant plastids. 1-Deoxy-D-xylulose 5-phosphate synthase (DXS) catalyzes the first and the rate-limiting step of the mevalonate-independent pathway and is an attractive target for the development of novel antibiotics, antimalarials, and herbicides. We report here the first structural information on DXS, from Escherichia coli and Deinococcus radiodurans, in complex with the coenzyme thiamine pyrophosphate (TPP). The structure contains three domains (I, II, and III), each of which bears homology to the equivalent domains in transketolase and the E1 subunit of pyruvate dehydrogenase. However, DXS has a novel arrangement of these domains as compared with the other enzymes, such that the active site of DXS is located at the interface of domains I and II in the same monomer, whereas that of transketolase is located at the interface of the dimer. The coenzyme TPP is mostly buried in the complex, but the C-2 atom of its thiazolium ring is exposed to a pocket that is the substrate-binding site. The structures identify residues that may have important roles in catalysis, which have been confirmed by our mutagenesis studies.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_17135236}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 17135236 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_17135236}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 31: |
Line 35: |
| | [[Category: Isoprenoid]] | | [[Category: Isoprenoid]] |
| | [[Category: Thiamine]] | | [[Category: Thiamine]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 10:12:16 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 23:10:48 2008'' |
Revision as of 20:10, 28 July 2008
Template:STRUCTURE 2o1s
1-deoxy-D-xylulose 5-phosphate synthase (DXS) from Escherichia coli
Template:ABSTRACT PUBMED 17135236
About this Structure
2O1S is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Crystal structure of 1-deoxy-D-xylulose 5-phosphate synthase, a crucial enzyme for isoprenoids biosynthesis., Xiang S, Usunow G, Lange G, Busch M, Tong L, J Biol Chem. 2007 Jan 26;282(4):2676-82. Epub 2006 Nov 29. PMID:17135236
Page seeded by OCA on Mon Jul 28 23:10:48 2008
