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1lw7
From Proteopedia
(New page: 200px<br /><applet load="1lw7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lw7, resolution 2.90Å" /> '''NADR PROTEIN FROM HA...) |
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| - | [[Image:1lw7.jpg|left|200px]]<br /><applet load="1lw7" size=" | + | [[Image:1lw7.jpg|left|200px]]<br /><applet load="1lw7" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1lw7, resolution 2.90Å" /> | caption="1lw7, resolution 2.90Å" /> | ||
'''NADR PROTEIN FROM HAEMOPHILUS INFLUENZAE'''<br /> | '''NADR PROTEIN FROM HAEMOPHILUS INFLUENZAE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Haemophilus influenzae NadR protein (hiNadR) has been shown to be a | + | 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== | ==About this Structure== | ||
| - | 1LW7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae] with SO4 and NAD as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1LW7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=NAD:'>NAD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LW7 OCA]. |
==Reference== | ==Reference== | ||
| Line 14: | Line 14: | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Chen, B.]] | [[Category: Chen, B.]] | ||
| - | [[Category: Grishin, N | + | [[Category: Grishin, N V.]] |
| - | [[Category: Kurnasov, O | + | [[Category: Kurnasov, O V.]] |
| - | [[Category: Osterman, A | + | [[Category: Osterman, A L.]] |
[[Category: Robinson, H.]] | [[Category: Robinson, H.]] | ||
| - | [[Category: Singh, S | + | [[Category: Singh, S K.]] |
[[Category: Zhang, H.]] | [[Category: Zhang, H.]] | ||
[[Category: NAD]] | [[Category: NAD]] | ||
| Line 27: | Line 27: | ||
[[Category: ribosylnicotinamide kinase]] | [[Category: ribosylnicotinamide kinase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:49:05 2008'' |
Revision as of 11:49, 21 February 2008
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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 with and as ligands. 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
Page seeded by OCA on Thu Feb 21 13:49:05 2008
