2n0m
From Proteopedia
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| - | ''' | + | ==The solution structure of the soluble form of the Lipid-modified Azurin from Neisseria gonorrhoeae== |
| + | <StructureSection load='2n0m' size='340' side='right' caption='[[2n0m]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2n0m]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2N0M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2N0M FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU1:COPPER+(I)+ION'>CU1</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2n0m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n0m OCA], [http://pdbe.org/2n0m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2n0m RCSB], [http://www.ebi.ac.uk/pdbsum/2n0m PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Neisseria gonorrhoeae colonizes the genitourinary track, and in these environments, especially in the female host, the bacteria are subjected to low levels of oxygen, and reactive oxygen and nitrosyl species. Here, the biochemical characterization of N. gonorrhoeae Laz is presented, as well as, the solution structure of its soluble domain determined by NMR. N. gonorrhoeae Laz is a type 1 copper protein of the azurin-family based on its spectroscopic properties and structure, with a redox potential of 277+/-5mV, at pH7.0, that behaves as a monomer in solution. The globular Laz soluble domain adopts the Greek-key motif, with the copper center located at one end of the beta-barrel coordinated by Gly48, His49, Cys113, His118 and Met122, in a distorted trigonal geometry. The edge of the His118 imidazole ring is water exposed, in a surface that is proposed to be involved in the interaction with its redox partners. The heterologously expressed Laz was shown to be a competent electron donor to N. gonorrhoeae cytochrome c peroxidase. This is an evidence for its involvement in the mechanism of protection against hydrogen peroxide generated by neighboring lactobacilli in the host environment. | ||
| - | The | + | The solution structure of the soluble form of the lipid-modified azurin from Neisseria gonorrhoeae, the electron donor of cytochrome c peroxidase.,Nobrega CS, Saraiva IH, Carreira C, Devreese B, Matzapetakis M, Pauleta SR Biochim Biophys Acta. 2016 Feb;1857(2):169-76. doi: 10.1016/j.bbabio.2015.11.006., Epub 2015 Nov 14. PMID:26589091<ref>PMID:26589091</ref> |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 2n0m" style="background-color:#fffaf0;"></div> | |
| - | + | == References == | |
| - | + | <references/> | |
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Carreira, C]] | [[Category: Carreira, C]] | ||
| - | [[Category: Matzapetakis, M | + | [[Category: Matzapetakis, M F]] |
| - | [[Category: Nobrega, C | + | [[Category: Nobrega, C F]] |
| - | [[Category: Pauleta, S | + | [[Category: Pauleta, S R]] |
| + | [[Category: Saraiva, I H]] | ||
| + | [[Category: Azurin-family]] | ||
| + | [[Category: Copper protein]] | ||
| + | [[Category: Electron transfer]] | ||
| + | [[Category: Metal binding protein]] | ||
| + | [[Category: Neisseria]] | ||
Revision as of 16:54, 20 January 2016
The solution structure of the soluble form of the Lipid-modified Azurin from Neisseria gonorrhoeae
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