1lw7
From Proteopedia
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- | [[Image:1lw7.jpg|left|200px]] | + | [[Image:1lw7.jpg|left|200px]] |
- | + | ||
- | '''NADR PROTEIN FROM HAEMOPHILUS INFLUENZAE''' | + | {{Structure |
+ | |PDB= 1lw7 |SIZE=350|CAPTION= <scene name='initialview01'>1lw7</scene>, resolution 2.90Å | ||
+ | |SITE= | ||
+ | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene> | ||
+ | |ACTIVITY= | ||
+ | |GENE= NadR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=727 Haemophilus influenzae]) | ||
+ | }} | ||
+ | |||
+ | '''NADR PROTEIN FROM HAEMOPHILUS INFLUENZAE''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1LW7 is a [ | + | 1LW7 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LW7 OCA]. |
==Reference== | ==Reference== | ||
- | Crystal structure of Haemophilus influenzae NadR protein. A bifunctional enzyme endowed with NMN adenyltransferase and ribosylnicotinimide kinase activities., Singh SK, Kurnasov OV, Chen B, Robinson H, Grishin NV, Osterman AL, Zhang H, J Biol Chem. 2002 Sep 6;277(36):33291-9. Epub 2002 Jun 14. PMID:[http:// | + | Crystal structure of Haemophilus influenzae NadR protein. A bifunctional enzyme endowed with NMN adenyltransferase and ribosylnicotinimide kinase activities., Singh SK, Kurnasov OV, Chen B, Robinson H, Grishin NV, Osterman AL, Zhang H, J Biol Chem. 2002 Sep 6;277(36):33291-9. Epub 2002 Jun 14. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12068016 12068016] |
[[Category: Haemophilus influenzae]] | [[Category: Haemophilus influenzae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: ribosylnicotinamide kinase]] | [[Category: ribosylnicotinamide kinase]] | ||
- | ''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 12:35:56 2008'' |
Revision as of 10:35, 20 March 2008
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, resolution 2.90Å | |||||||
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Ligands: | and | ||||||
Gene: | NadR (Haemophilus influenzae) | ||||||
Coordinates: | save as pdb, mmCIF, xml |
NADR PROTEIN FROM HAEMOPHILUS INFLUENZAE
Overview
Haemophilus influenzae NadR protein (hiNadR) has been shown to be a bifunctional enzyme possessing both NMN adenylytransferase (NMNAT; EC ) and ribosylnicotinamide kinase (RNK; EC ) activities. Its function is essential for the growth and survival of H. influenzae and thus may present a new highly specific anti-infectious drug target. We have solved the crystal structure of hiNadR complexed with NAD using the selenomethionine MAD phasing method. The structure reveals the presence of two distinct domains. The N-terminal domain that hosts the NMNAT activity is closely related to archaeal NMNAT, whereas the C-terminal domain, which has been experimentally demonstrated to possess ribosylnicotinamide kinase activity, is structurally similar to yeast thymidylate kinase and several other P-loop-containing kinases. There appears to be no cross-talk between the two active sites. The bound NAD at the active site of the NMNAT domain reveals several critical interactions between NAD and the protein. There is also a second non-active-site NAD molecule associated with the C-terminal RNK domain that adopts a highly folded conformation with the nicotinamide ring stacking over the adenine base. Whereas the RNK domain of the hiNadR structure presented here is the first structural characterization of a ribosylnicotinamide kinase from any organism, the NMNAT domain of hiNadR defines yet another member of the pyridine nucleotide adenylyltransferase family.
About this Structure
1LW7 is a Single protein structure of sequence from Haemophilus influenzae. Full crystallographic information is available from OCA.
Reference
Crystal structure of Haemophilus influenzae NadR protein. A bifunctional enzyme endowed with NMN adenyltransferase and ribosylnicotinimide kinase activities., Singh SK, Kurnasov OV, Chen B, Robinson H, Grishin NV, Osterman AL, Zhang H, J Biol Chem. 2002 Sep 6;277(36):33291-9. Epub 2002 Jun 14. PMID:12068016
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