|
|
| Line 1: |
Line 1: |
| | | | |
| | ==Crystal structure of NreA of Staphylococcus carnosus with bound nitrate== | | ==Crystal structure of NreA of Staphylococcus carnosus with bound nitrate== |
| - | <StructureSection load='4iuk' size='340' side='right' caption='[[4iuk]], [[Resolution|resolution]] 2.35Å' scene=''> | + | <StructureSection load='4iuk' size='340' side='right'caption='[[4iuk]], [[Resolution|resolution]] 2.35Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4iuk]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Stact Stact]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IUK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4IUK FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4iuk]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_carnosus_subsp._carnosus_TM300 Staphylococcus carnosus subsp. carnosus TM300]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IUK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4IUK FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">nreA, Sca_1890, SCA_1890 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=396513 STACT])</td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4iuk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4iuk OCA], [https://pdbe.org/4iuk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4iuk RCSB], [https://www.ebi.ac.uk/pdbsum/4iuk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4iuk ProSAT]</span></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=4iuk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4iuk OCA], [http://pdbe.org/4iuk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4iuk RCSB], [http://www.ebi.ac.uk/pdbsum/4iuk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4iuk ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/B9DL91_STACT B9DL91_STACT] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 21: |
Line 22: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Stact]] | + | [[Category: Large Structures]] |
| - | [[Category: Niemann, V]] | + | [[Category: Staphylococcus carnosus subsp. carnosus TM300]] |
| - | [[Category: Stehle, T]] | + | [[Category: Niemann V]] |
| - | [[Category: Cytosolic]] | + | [[Category: Stehle T]] |
| - | [[Category: Gaf domain]]
| + | |
| - | [[Category: Nitrate]]
| + | |
| - | [[Category: Nitrate binding]]
| + | |
| - | [[Category: Nitrate sensor]]
| + | |
| - | [[Category: Nitrate-binding protein]]
| + | |
| - | [[Category: Staphylococcus]]
| + | |
| Structural highlights
Function
B9DL91_STACT
Publication Abstract from PubMed
Staphylococci are able to use nitrate as an alternative electron acceptor during anaerobic respiration. The regulation of energy metabolism is dependent on the presence of oxygen and nitrate. Under anaerobic conditions, staphylococci employ the nitrate regulatory element (Nre) for transcriptional activation of genes involved in reduction and transport of nitrate and nitrite. Of the three proteins that constitute the Nre system, NreB has been characterized as an oxygen sensor kinase and NreC has been characterized as its cognate response regulator. Here, we present structural and functional data that establish NreA as a new type of nitrate receptor. The structure of NreA with bound nitrate was solved at 2.35A resolution, revealing a GAF domain fold. Isothermal titration calorimetry experiments showed that NreA binds nitrate with low micromolar affinity (KD=22muM). Two crystal forms for NreA were obtained, with either bound nitrate or iodide. While the binding site is hydrophobic, two helix dipoles and polar interactions contribute to specific binding of the ions. The expression of nitrate reductase (NarGHI) was examined using a narG-lip (lipase) reporter gene assay in vivo. Expression was regulated by the presence of NreA and nitrate. Structure-guided mutations of NreA reduced its nitrate binding affinity and also affected the gene expression, thus providing support for the function of NreA as a nitrate receptor.
The NreA Protein Functions as a Nitrate Receptor in the Staphylococcal Nitrate Regulation System.,Niemann V, Koch-Singenstreu M, Neu A, Nilkens S, Gotz F, Unden G, Stehle T J Mol Biol. 2013 Dec 31. pii: S0022-2836(13)00813-9. doi:, 10.1016/j.jmb.2013.12.026. PMID:24389349[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Niemann V, Koch-Singenstreu M, Neu A, Nilkens S, Gotz F, Unden G, Stehle T. The NreA Protein Functions as a Nitrate Receptor in the Staphylococcal Nitrate Regulation System. J Mol Biol. 2013 Dec 31. pii: S0022-2836(13)00813-9. doi:, 10.1016/j.jmb.2013.12.026. PMID:24389349 doi:http://dx.doi.org/10.1016/j.jmb.2013.12.026
|
