1od6: Difference between revisions
No edit summary |
No edit summary |
||
Line 1: | Line 1: | ||
[[Image:1od6.jpg|left|200px]] | [[Image:1od6.jpg|left|200px]] | ||
'''THE CRYSTAL STRUCTURE OF PHOSPHOPANTETHEINE ADENYLYLTRANSFERASE FROM THERMUS THERMOPHILUS IN COMPLEX WITH 4'-PHOSPHOPANTETHEINE''' | {{Structure | ||
|PDB= 1od6 |SIZE=350|CAPTION= <scene name='initialview01'>1od6</scene>, resolution 1.5Å | |||
|SITE= <scene name='pdbsite=AC1:So4+Binding+Site+For+Chain+A'>AC1</scene> | |||
|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=PNS:4'-PHOSPHOPANTETHEINE'>PNS</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Pantetheine-phosphate_adenylyltransferase Pantetheine-phosphate adenylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.3 2.7.7.3] | |||
|GENE= | |||
}} | |||
'''THE CRYSTAL STRUCTURE OF PHOSPHOPANTETHEINE ADENYLYLTRANSFERASE FROM THERMUS THERMOPHILUS IN COMPLEX WITH 4'-PHOSPHOPANTETHEINE''' | |||
==Overview== | ==Overview== | ||
Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
1OD6 is a [ | 1OD6 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OD6 OCA]. | ||
==Reference== | ==Reference== | ||
Structure and implications for the thermal stability of phosphopantetheine adenylyltransferase from Thermus thermophilus., Takahashi H, Inagaki E, Fujimoto Y, Kuroishi C, Nodake Y, Nakamura Y, Arisaka F, Yutani K, Kuramitsu S, Yokoyama S, Yamamoto M, Miyano M, Tahirov TH, Acta Crystallogr D Biol Crystallogr. 2004 Jan;60(Pt 1):97-104. Epub 2003, Dec 18. PMID:[http:// | Structure and implications for the thermal stability of phosphopantetheine adenylyltransferase from Thermus thermophilus., Takahashi H, Inagaki E, Fujimoto Y, Kuroishi C, Nodake Y, Nakamura Y, Arisaka F, Yutani K, Kuramitsu S, Yokoyama S, Yamamoto M, Miyano M, Tahirov TH, Acta Crystallogr D Biol Crystallogr. 2004 Jan;60(Pt 1):97-104. Epub 2003, Dec 18. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14684898 14684898] | ||
[[Category: Pantetheine-phosphate adenylyltransferase]] | [[Category: Pantetheine-phosphate adenylyltransferase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
Line 25: | Line 34: | ||
[[Category: riken structural genomics/proteomics initiative]] | [[Category: riken structural genomics/proteomics initiative]] | ||
[[Category: rsgi]] | [[Category: rsgi]] | ||
[[Category: structural | [[Category: structural genomic]] | ||
[[Category: transferase]] | [[Category: transferase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:09:11 2008'' |
Revision as of 14:09, 20 March 2008
| |||||||
, resolution 1.5Å | |||||||
---|---|---|---|---|---|---|---|
Sites: | |||||||
Ligands: | and | ||||||
Activity: | Pantetheine-phosphate adenylyltransferase, with EC number 2.7.7.3 | ||||||
Coordinates: | save as pdb, mmCIF, xml |
THE CRYSTAL STRUCTURE OF PHOSPHOPANTETHEINE ADENYLYLTRANSFERASE FROM THERMUS THERMOPHILUS IN COMPLEX WITH 4'-PHOSPHOPANTETHEINE
OverviewOverview
Phosphopantetheine adenylyltransferase (PPAT) is an essential enzyme in bacteria that catalyzes the rate-limiting step in coenzyme A (CoA) biosynthesis by transferring an adenylyl group from ATP to 4'-phosphopantetheine (Ppant), yielding 3'-dephospho-CoA (dPCoA). The crystal structure of PPAT from Thermus thermophilus HB8 (Tt PPAT) complexed with Ppant has been determined by the molecular-replacement method at 1.5 A resolution. The overall fold of the enzyme is almost the same as that of Escherichia coli PPAT, a hexamer having point group 32. The asymmetric unit of Tt PPAT contains a monomer and the crystallographic triad and dyad coincide with the threefold and twofold axes of the hexamer, respectively. Most of the important atoms surrounding the active site in E. coli PPAT are conserved in Tt PPAT, indicating similarities in their substrate binding and enzymatic reaction. The notable difference between E. coli PPAT and Tt PPAT is the simultaneous substrate recognition by all six subunits of Tt PPAT compared with substrate recognition by only three subunits in E. coli PPAT. Comparative analysis also revealed that the higher stability of Tt PPAT arises from stabilization of each subunit by hydrophobic effects, hydrogen bonds and entropic effects.
About this StructureAbout this Structure
1OD6 is a Single protein structure of sequence from Thermus thermophilus. Full crystallographic information is available from OCA.
ReferenceReference
Structure and implications for the thermal stability of phosphopantetheine adenylyltransferase from Thermus thermophilus., Takahashi H, Inagaki E, Fujimoto Y, Kuroishi C, Nodake Y, Nakamura Y, Arisaka F, Yutani K, Kuramitsu S, Yokoyama S, Yamamoto M, Miyano M, Tahirov TH, Acta Crystallogr D Biol Crystallogr. 2004 Jan;60(Pt 1):97-104. Epub 2003, Dec 18. PMID:14684898
Page seeded by OCA on Thu Mar 20 13:09:11 2008
Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Pages with broken file links
- Pantetheine-phosphate adenylyltransferase
- Single protein
- Thermus thermophilus
- Inagaki, E.
- Miyano, M.
- RSGI, RIKEN Structural Genomics/Proteomics Initiative.
- Tahirov, T.
- Takahashi, H.
- PNS
- SO4
- Coenzyme a biosynthesis
- Nucleotidyltransferase
- Riken structural genomics/proteomics initiative
- Rsgi
- Structural genomic
- Transferase