View source for 3tfg


==Crystal structure of an H-NOX protein from Nostoc sp. PCC 7120, L66W/L67W double mutant==
<StructureSection load='3tfg' size='340' side='right'caption='[[3tfg]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3tfg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Nostoc_sp._PCC_7120_=_FACHB-418 Nostoc sp. PCC 7120 = FACHB-418]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TFG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TFG FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9003&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=MLA:MALONIC+ACID'>MLA</scene></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=3tfg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tfg OCA], [https://pdbe.org/3tfg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tfg RCSB], [https://www.ebi.ac.uk/pdbsum/3tfg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tfg ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q8YUQ7_NOSS1 Q8YUQ7_NOSS1] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Interior topological features, such as pockets and channels, have evolved in proteins to regulate biological functions by facilitating the diffusion of biomolecules. Decades of research using the globins as model heme proteins have clearly highlighted the importance of gas pockets around the heme in controlling the capture and release of O(2). However, much less is known about how ligand migration contributes to the diverse functions of other heme protein scaffolds. Heme nitric oxide/oxygen binding (H-NOX) domains are a conserved family of gas-sensing heme proteins with a divergent fold that are critical to numerous signaling pathways. Utilizing X-ray crystallography with xenon, a tunnel network has been shown to serve as a molecular pathway for ligand diffusion. Structure-guided mutagenesis results show that the tunnels have unexpected effects on gas-sensing properties in H-NOX domains. The findings provide insights on how the flux of biomolecules through protein scaffolds modulates protein chemistry.

Tunnels modulate ligand flux in a heme nitric oxide/oxygen binding (H-NOX) domain.,Winter MB, Herzik MA Jr, Kuriyan J, Marletta MA Proc Natl Acad Sci U S A. 2011 Oct 25;108(43):E881-9. Epub 2011 Oct 12. PMID:21997213<ref>PMID:21997213</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3tfg" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Nostoc sp. PCC 7120 = FACHB-418]]
[[Category: Herzik Jr MA]]
[[Category: Kuriyan J]]
[[Category: Marletta MA]]
[[Category: Winter MB]]