1kbv
From Proteopedia
(New page: 200px<br /><applet load="1kbv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kbv, resolution 1.95Å" /> '''NITRITE-SOAKED CRYST...) |
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| - | [[Image:1kbv.jpg|left|200px]]<br /><applet load="1kbv" size=" | + | [[Image:1kbv.jpg|left|200px]]<br /><applet load="1kbv" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1kbv, resolution 1.95Å" /> | caption="1kbv, resolution 1.95Å" /> | ||
'''NITRITE-SOAKED CRYSTAL STRUCTURE OF THE SOLUBLE DOMAIN OF ANIA FROM NEISSERIA GONORRHOEAE'''<br /> | '''NITRITE-SOAKED CRYSTAL STRUCTURE OF THE SOLUBLE DOMAIN OF ANIA FROM NEISSERIA GONORRHOEAE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The major anaerobically induced outer membrane protein (AniA) from | + | The major anaerobically induced outer membrane protein (AniA) from pathogenic Neisseria gonorrhoeae is essential for cell growth under oxygen limiting conditions in the presence of nitrite and is protective against killing by human sera. A phylogenic analysis indicates that AniA is a member of a new class of copper-containing nitrite reductases. Expression of the soluble domain of AniA yields a protein capable of reducing nitrite with specific activity of 160 units/mg, approximately 50 % of that measured for the nitrite reductase from the strong soil denitrifier Alcaligenes faecalis S-6. The crystal structure of the soluble domain of AniA was solved by molecular replacement and sixfold averaging to a resolution of 2.4 A. The nitrite soaked AniA crystal structure refined to 1.95 A reveals a bidentate mode of substrate binding to the type II copper. Despite low sequence identity (approximately 30 %), the core cupredoxin fold of AniA is similar to that found in copper-containing nitrite reductases from soil bacteria. The main structural differences are localized to two attenuated surface loops that map to deletions in the sequence alignment. In soil nitrite reductases, one of these surface loops is positioned near the type I copper site and contributes residues to the docking surface for proteaceous electron donors. In AniA, the attenuation of this loop results in a restructured hydrophobic binding surface that may be required to interact with a lipid anchored azurin. The second attenuated loop is positioned on the opposite side of AniA and may facilitate a more intimate interaction with the lipid membrane. A unique combination of structural effectors surrounding the type I copper site of sAnia contribute to a unusual visible absorption spectra with components observed previously in either green or blue type I copper sites. |
==About this Structure== | ==About this Structure== | ||
| - | 1KBV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Neisseria_gonorrhoeae Neisseria gonorrhoeae] with CU and NO2 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1KBV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Neisseria_gonorrhoeae Neisseria gonorrhoeae] with <scene name='pdbligand=CU:'>CU</scene> and <scene name='pdbligand=NO2:'>NO2</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KBV OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Neisseria gonorrhoeae]] | [[Category: Neisseria gonorrhoeae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Boulanger, M | + | [[Category: Boulanger, M J.]] |
| - | [[Category: Murphy, M | + | [[Category: Murphy, M E.P.]] |
[[Category: CU]] | [[Category: CU]] | ||
[[Category: NO2]] | [[Category: NO2]] | ||
[[Category: ania[no2-]]] | [[Category: ania[no2-]]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:32:20 2008'' |
Revision as of 11:32, 21 February 2008
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NITRITE-SOAKED CRYSTAL STRUCTURE OF THE SOLUBLE DOMAIN OF ANIA FROM NEISSERIA GONORRHOEAE
Overview
The major anaerobically induced outer membrane protein (AniA) from pathogenic Neisseria gonorrhoeae is essential for cell growth under oxygen limiting conditions in the presence of nitrite and is protective against killing by human sera. A phylogenic analysis indicates that AniA is a member of a new class of copper-containing nitrite reductases. Expression of the soluble domain of AniA yields a protein capable of reducing nitrite with specific activity of 160 units/mg, approximately 50 % of that measured for the nitrite reductase from the strong soil denitrifier Alcaligenes faecalis S-6. The crystal structure of the soluble domain of AniA was solved by molecular replacement and sixfold averaging to a resolution of 2.4 A. The nitrite soaked AniA crystal structure refined to 1.95 A reveals a bidentate mode of substrate binding to the type II copper. Despite low sequence identity (approximately 30 %), the core cupredoxin fold of AniA is similar to that found in copper-containing nitrite reductases from soil bacteria. The main structural differences are localized to two attenuated surface loops that map to deletions in the sequence alignment. In soil nitrite reductases, one of these surface loops is positioned near the type I copper site and contributes residues to the docking surface for proteaceous electron donors. In AniA, the attenuation of this loop results in a restructured hydrophobic binding surface that may be required to interact with a lipid anchored azurin. The second attenuated loop is positioned on the opposite side of AniA and may facilitate a more intimate interaction with the lipid membrane. A unique combination of structural effectors surrounding the type I copper site of sAnia contribute to a unusual visible absorption spectra with components observed previously in either green or blue type I copper sites.
About this Structure
1KBV is a Single protein structure of sequence from Neisseria gonorrhoeae with and as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structure of the soluble domain of the major anaerobically induced outer membrane protein (AniA) from pathogenic Neisseria: a new class of copper-containing nitrite reductases., Boulanger MJ, Murphy ME, J Mol Biol. 2002 Feb 1;315(5):1111-27. PMID:11827480[[Category: ania[no2-]]]
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