1ytk
From Proteopedia
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'''Crystal structure of a nicotinate phosphoribosyltransferase from Thermoplasma acidophilum with nicotinate mononucleotide''' | '''Crystal structure of a nicotinate phosphoribosyltransferase from Thermoplasma acidophilum with nicotinate mononucleotide''' | ||
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[[Category: BSGC, Berkeley Structural Genomics Center.]] | [[Category: BSGC, Berkeley Structural Genomics Center.]] | ||
[[Category: Shin, D H.]] | [[Category: Shin, D H.]] | ||
| - | [[Category: | + | [[Category: Berkeley structural genomics center]] |
| - | [[Category: | + | [[Category: Bsgc]] |
| - | [[Category: | + | [[Category: Crystal structure]] |
| - | [[Category: | + | [[Category: Nicotinate phosphoribosyltransferase]] |
| - | [[Category: | + | [[Category: Protein structure initiative]] |
| - | [[Category: | + | [[Category: Psi]] |
| - | [[Category: | + | [[Category: Structural genomic]] |
| - | [[Category: | + | [[Category: Type ii phosphoribosyltransferase]] |
| - | [[Category: | + | [[Category: Zinc-knuckle motif]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 16:46:21 2008'' | |
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Revision as of 13:46, 3 May 2008
Crystal structure of a nicotinate phosphoribosyltransferase from Thermoplasma acidophilum with nicotinate mononucleotide
Overview
We have determined the crystal structure of nicotinate phosphoribosyltransferase from Themoplasma acidophilum (TaNAPRTase). The TaNAPRTase has three domains, an N-terminal domain, a central functional domain, and a unique C-terminal domain. The crystal structure revealed that the functional domain has a type II phosphoribosyltransferase fold that may be a common architecture for both nicotinic acid and quinolinic acid (QA) phosphoribosyltransferases (PRTase) despite low sequence similarity between them. Unlike QAPRTase, TaNAPRTase has a unique extra C-terminal domain containing a zinc knuckle-like motif containing 4 cysteines. The TaNAPRTase forms a trimer of dimers in the crystal. The active site pocket is formed at dimer interfaces. The complex structures with phosphoribosylpyrophosphate (PRPP) and nicotinate mononucleotide (NAMN) showed, surprisingly, that functional residues lining on the active site of TaNAPRTase are quite different from those of QAPRTase, although their substrates are quite similar to each other. The phosphate moiety of PRPP and NAMN is anchored to the phosphate-binding loops formed by backbone amides, as found in many alpha/beta barrel enzymes. The pyrophosphate moiety of PRPP is located at the entrance of the active site pocket, whereas the nicotinate moiety of NAMN is located deep inside. Interestingly, the nicotinate moiety of NAMN is intercalated between highly conserved aromatic residues Tyr(21) and Phe(138). Careful structural analyses combined with other NAPRTase sequence subfamilies reveal that TaNAPRTase represents a unique sequence subfamily of NAPRTase. The structures of TaNAPRTase also provide valuable insight for other sequence subfamilies such as pre-B cell colony-enhancing factor, known to have nicotinamide phosphoribosyltransferase activity.
About this Structure
1YTK is a Single protein structure of sequence from Thermoplasma acidophilum dsm 1728. Full crystallographic information is available from OCA.
Reference
Crystal structure of a nicotinate phosphoribosyltransferase from Thermoplasma acidophilum., Shin DH, Oganesyan N, Jancarik J, Yokota H, Kim R, Kim SH, J Biol Chem. 2005 May 6;280(18):18326-35. Epub 2005 Mar 6. PMID:15753098 Page seeded by OCA on Sat May 3 16:46:21 2008
Categories: Nicotinate phosphoribosyltransferase | Single protein | Thermoplasma acidophilum dsm 1728 | BSGC, Berkeley Structural Genomics Center. | Shin, D H. | Berkeley structural genomics center | Bsgc | Crystal structure | Protein structure initiative | Psi | Structural genomic | Type ii phosphoribosyltransferase | Zinc-knuckle motif
