3tfe: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older edit
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
 
(6 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:3tfe.jpg|left|200px]]


<!--
==Crystal structure of an H-NOX protein from Nostoc sp. PCC 7120, L66W mutant under 6 atm of xenon==
The line below this paragraph, containing "STRUCTURE_3tfe", creates the "Structure Box" on the page.
<StructureSection load='3tfe' size='340' side='right'caption='[[3tfe]], [[Resolution|resolution]] 1.99&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[3tfe]] 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=3TFE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TFE FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.991&#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>, <scene name='pdbligand=XE:XENON'>XE</scene></td></tr>
{{STRUCTURE_3tfe|  PDB=3tfe  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3tfe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tfe OCA], [https://pdbe.org/3tfe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tfe RCSB], [https://www.ebi.ac.uk/pdbsum/3tfe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tfe 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.


===Crystal structure of an H-NOX protein from Nostoc sp. PCC 7120, L66W mutant under 6 atm of xenon===
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>
The line below this paragraph, {{ABSTRACT_PUBMED_21997213}}, adds the Publication Abstract to the page
<div class="pdbe-citations 3tfe" style="background-color:#fffaf0;"></div>
(as it appears on PubMed at http://www.pubmed.gov), where 21997213 is the PubMed ID number.
== References ==
-->
<references/>
{{ABSTRACT_PUBMED_21997213}}
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Large Structures]]
[[3tfe]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Nostoc_sp. Nostoc sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TFE OCA].
[[Category: Nostoc sp. PCC 7120 = FACHB-418]]
 
[[Category: Herzik Jr MA]]
==Reference==
[[Category: Kuriyan J]]
<ref group="xtra">PMID:021997213</ref><references group="xtra"/>
[[Category: Marletta MA]]
[[Category: Nostoc sp.]]
[[Category: Winter MB]]
[[Category: Herzik, M A.]]
[[Category: Kuriyan, J.]]
[[Category: Marletta, M A.]]
[[Category: Winter, M B.]]
[[Category: Gas binding]]
[[Category: Heme-based sensor domain]]
[[Category: Signaling protein]]

Latest revision as of 10:19, 13 August 2026

Crystal structure of an H-NOX protein from Nostoc sp. PCC 7120, L66W mutant under 6 atm of xenon

3tfe, resolution 1.99Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=3tfe&oldid=4478411"