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3ag5
From Proteopedia
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| - | [[Image:3ag5.png|left|200px]] | ||
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{{STRUCTURE_3ag5| PDB=3ag5 | SCENE= }} | {{STRUCTURE_3ag5| PDB=3ag5 | SCENE= }} | ||
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===Crystal Structure of Pantothenate Synthetase from Staphylococcus aureus=== | ===Crystal Structure of Pantothenate Synthetase from Staphylococcus aureus=== | ||
| + | {{ABSTRACT_PUBMED_20568730}} | ||
| - | + | ==Function== | |
| + | [[http://www.uniprot.org/uniprot/PANC_STAA8 PANC_STAA8]] Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate (By similarity). | ||
==About this Structure== | ==About this Structure== | ||
| - | [[3ag5]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ | + | [[3ag5]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus_nctc_8325 Staphylococcus aureus subsp. aureus nctc 8325]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AG5 OCA]. |
==See Also== | ==See Also== | ||
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==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID:020568730</ref><references group="xtra"/> | + | <ref group="xtra">PMID:020568730</ref><references group="xtra"/><references/> |
[[Category: Pantoate--beta-alanine ligase]] | [[Category: Pantoate--beta-alanine ligase]] | ||
| - | [[Category: Staphylococcus aureus]] | + | [[Category: Staphylococcus aureus subsp. aureus nctc 8325]] |
[[Category: Inoue, T.]] | [[Category: Inoue, T.]] | ||
[[Category: Konishi, S.]] | [[Category: Konishi, S.]] | ||
Revision as of 08:46, 4 September 2013
Contents |
Crystal Structure of Pantothenate Synthetase from Staphylococcus aureus
Template:ABSTRACT PUBMED 20568730
Function
[PANC_STAA8] Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate (By similarity).
About this Structure
3ag5 is a 2 chain structure with sequence from Staphylococcus aureus subsp. aureus nctc 8325. Full crystallographic information is available from OCA.
See Also
Reference
- Satoh A, Konishi S, Tamura H, Stickland HG, Whitney HM, Smith AG, Matsumura H, Inoue T. Substrate-Induced Closing of the Active Site Revealed by the Crystal Structure of Pantothenate Synthetase from Staphylococcus aureus. Biochemistry. 2010 Jul 8. PMID:20568730 doi:10.1021/bi1004206
Categories: Pantoate--beta-alanine ligase | Staphylococcus aureus subsp. aureus nctc 8325 | Inoue, T. | Konishi, S. | Matsumura, H. | Satoh, A. | Smith, A G. | Stickland, H G. | Tamura, H. | Whitney, H M. | Atp-binding | Atp-dependent enzyme | Ligase | Nucleotide-binding | Open/close mechanism | Pantothenate biosynthesis | Pantothenate synthetase
