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| [[Image:1ih8.gif|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1ih8| PDB=1ih8 | SCENE= }} | | {{STRUCTURE_1ih8| PDB=1ih8 | SCENE= }} |
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| '''NH3-dependent NAD+ Synthetase from Bacillus subtilis Complexed with AMP-CPP and Mg2+ ions.'''
| | ===NH3-dependent NAD+ Synthetase from Bacillus subtilis Complexed with AMP-CPP and Mg2+ ions.=== |
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| ==Overview==
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| The NH(3)-dependent NAD(+) synthetase (NADS) participates in the biosynthesis of nicotinamide adenine dinucleotide (NAD(+)) by transforming nicotinic acid adenine dinucleotide (NaAD) to NAD(+). The structural behavior of the active site, including stabilization of flexible loops 82-87 and 204-225, has been studied by determination of the crystal structures of complexes of NADS with natural substrates and a substrate analog. Both loops are stabilized independently of NaAD and solely from the ATP-binding site. Analysis of the binding contacts suggests that the minor loop 82-87 is stabilized primarily by a hydrogen bond with the adenine base of ATP. Formation of a coordination complex with Mg(2+) in the ATP-binding site may contribute to the stabilization of the major loop 204-225. The major loop has a role in substrate recognition and stabilization, in addition to the protection of the reaction intermediate described previously. A second and novel Mg(2+) position has been observed closer to the NaAD-binding site in the structure crystallized at pH 7.5, where the enzyme is active. This could therefore be the catalytically active Mg(2+). | | The line below this paragraph, {{ABSTRACT_PUBMED_11375500}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 11375500 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_11375500}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Atp pyrophosphatase]] | | [[Category: Atp pyrophosphatase]] |
| [[Category: Ligase]] | | [[Category: Ligase]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:59:47 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 12:10:30 2008'' |