ATP binding domain 4 Functions: Difference between revisions
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- Usually ATP-pyrophosphatatse has a domain of GMP synthetase, for adding adenine and help lysine attack on Carbon atom. | - Usually ATP-pyrophosphatatse has a domain of GMP synthetase, for adding adenine and help lysine attack on Carbon atom. | ||
http://www.pnas.org/content/102/21/7487.abstract | http://www.pnas.org/content/102/21/7487.abstract | ||
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- NAD+ synthetase belongs to a member of the family of N-type ATP pyrophosphatase (ATP PPases) | |||
- Some other members of N-type ATP pyrophosphatase include NAD+ synthetase, GMP synthetase, asparagine synthetase and argininosuccinate synthetase | |||
- this family is characterised by strictly conserved fingerprint sequence Ser-Gly-Gly-X-Ser/ Thr-Ser/ Thr at P-loop (this is found by the comparison of 3-D structures of NAD+ synthetase and GMP synthetase | |||
- Since they are in the same family, we can infer their structure similarities and propose the functions of our sequences. | |||
- Look for the ATP-binding sites on ref[11] | |||
- Rizzi, M., et al., & Galizzi, A. (1996). Crystal structure of NH3-dependent NAD synthetase from Bacillus subtilis. EMBO J. 15, 5125-5134 | |||
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Revision as of 07:16, 19 May 2009
ATP Binding domain 4 proteins - shows little homology with human protein, and the % sequence ID = 36.8% - under the family of AAHN-like super family
My sequences:
putative n-type ATP pyrophosphatase from Pyrococcus furiosus, the Northeast Structural Genomics Target PfR23
- ATP pyrophosphatase (ATP PPase) is used to assist lysidine formation using a lysine-specific loop and tRNA recognition domain - Lysidine is a lysine-combined modified cytidine, locating at antcodon wobble position (34) of bacterial tRNA - Usually ATP-pyrophosphatatse has a domain of GMP synthetase, for adding adenine and help lysine attack on Carbon atom. http://www.pnas.org/content/102/21/7487.abstract
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- NAD+ synthetase belongs to a member of the family of N-type ATP pyrophosphatase (ATP PPases) - Some other members of N-type ATP pyrophosphatase include NAD+ synthetase, GMP synthetase, asparagine synthetase and argininosuccinate synthetase - this family is characterised by strictly conserved fingerprint sequence Ser-Gly-Gly-X-Ser/ Thr-Ser/ Thr at P-loop (this is found by the comparison of 3-D structures of NAD+ synthetase and GMP synthetase - Since they are in the same family, we can infer their structure similarities and propose the functions of our sequences. - Look for the ATP-binding sites on ref[11] - Rizzi, M., et al., & Galizzi, A. (1996). Crystal structure of NH3-dependent NAD synthetase from Bacillus subtilis. EMBO J. 15, 5125-5134
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