5jrx

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m (Protected "5jrx" [edit=sysop:move=sysop])
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'''Unreleased structure'''
 
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The entry 5jrx is ON HOLD until Paper Publication
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==Crystal structure of Fe(II) CO-bound H-NOX protein from C. subterraneus==
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<StructureSection load='5jrx' size='340' side='right' caption='[[5jrx]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5jrx]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JRX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5JRX FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CMO:CARBON+MONOXIDE'>CMO</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5jrv|5jrv]], [[5jru|5jru]]</td></tr>
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<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=5jrx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jrx OCA], [http://pdbe.org/5jrx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jrx RCSB], [http://www.ebi.ac.uk/pdbsum/5jrx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jrx ProSAT]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Acute and specific sensing of diatomic gas molecules is an essential facet of biological signaling. Heme nitric oxide/oxygen binding (H-NOX) proteins are a family of gas sensors found in diverse classes of bacteria and eukaryotes. The most commonly characterized bacterial H-NOX domains are from facultative anaerobes and are activated through a conformational change caused by formation of a 5-coordinate Fe(II)-NO complex. Members of this H-NOX subfamily do not bind O2 and therefore can selectively ligate NO even under aerobic conditions. In contrast, H-NOX domains encoded by obligate anaerobes do form stable 6-coordinate Fe(II)-O2 complexes by utilizing a conserved H-bonding network in the ligand-binding pocket. The biological function of O2-binding H-NOX domains has not been characterized. In this work, the crystal structures of an O2-binding H-NOX domain from the thermophilic obligate anaerobe Caldanaerobacter subterraneus (Cs H-NOX) in the Fe(II)-NO, Fe(II)-CO, and Fe(II)-unliganded states are reported. The Fe(II)-unliganded structure displays a conformational shift distinct from the NO-, CO-, and previously reported O2-coordinated structures. In orthogonal signaling assays using Cs H-NOX and the H-NOX signaling effector histidine kinase from Vibrio cholerae (Vc HnoK), Cs H-NOX regulates Vc HnoK in an O2-dependent manner and requires the H-bonding network to distinguish O2 from other ligands. The crystal structures of Fe(II) unliganded and NO- and CO-bound Cs H-NOX combined with functional assays herein provide the first evidence that H-NOX proteins from obligate anaerobes can serve as O2 sensors.
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Authors: Bruegger, J., Hespen, C., Phillips-Piro, C.M., Marletta, M.A.
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Structural and Functional Evidence Indicates Selective Oxygen Signaling in Caldanaerobacter subterraneus H-NOX.,Hespen CW, Bruegger JJ, Phillips-Piro CM, Marletta MA ACS Chem Biol. 2016 Jun 30. PMID:27328180<ref>PMID:27328180</ref>
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Description: Crystal structure of Fe(II) CO-bound H-NOX protein from C. subterraneus
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Phillips-Piro, C.M]]
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<div class="pdbe-citations 5jrx" style="background-color:#fffaf0;"></div>
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[[Category: Marletta, M.A]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Bruegger, J]]
[[Category: Bruegger, J]]
[[Category: Hespen, C]]
[[Category: Hespen, C]]
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[[Category: Marletta, M A]]
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[[Category: Phillips-Piro, C M]]
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[[Category: Gas binding]]
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[[Category: Heme-based methyl-accepting chemotaxis protein]]
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[[Category: Signaling protein]]

Revision as of 02:18, 13 July 2016

Crystal structure of Fe(II) CO-bound H-NOX protein from C. subterraneus

5jrx, resolution 1.95Å

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