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==I5F Mutant Structure of T. Tengcongensis H-NOX==
==I5F Mutant Structure of T. Tengcongensis H-NOX==
<StructureSection load='3sj5' size='340' side='right' caption='[[3sj5]], [[Resolution|resolution]] 1.67&Aring;' scene=''>
<StructureSection load='3sj5' size='340' side='right'caption='[[3sj5]], [[Resolution|resolution]] 1.67&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3sj5]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Caldanaerobacter_subterraneus Caldanaerobacter subterraneus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SJ5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3SJ5 FirstGlance]. <br>
<table><tr><td colspan='2'>[[3sj5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Caldanaerobacter_subterraneus_subsp._tengcongensis Caldanaerobacter subterraneus subsp. tengcongensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SJ5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SJ5 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.673&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1u55|1u55]], [[1u4h|1u4h]], [[1u56|1u56]], [[3eee|3eee]], [[3iqb|3iqb]], [[3lah|3lah]], [[3lai|3lai]]</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></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Tar4, TTE0680 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=911092 Caldanaerobacter subterraneus])</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=3sj5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sj5 OCA], [https://pdbe.org/3sj5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3sj5 RCSB], [https://www.ebi.ac.uk/pdbsum/3sj5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3sj5 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=3sj5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sj5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3sj5 RCSB], [http://www.ebi.ac.uk/pdbsum/3sj5 PDBsum]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/Q8RBX6_CALS4 Q8RBX6_CALS4]
Heme Nitric oxide/OXygen binding (H-NOX) domains have provided a novel scaffold to probe ligand affinity in hemoproteins. Mutation of isoleucine 5, a conserved residue located in the heme-binding pocket of the H-NOX domain from Thermoanaerobacter tengcongensis (Tt H-NOX), was carried out to examine changes in oxygen (O(2))-binding properties. A series of I5 mutants (I5F, I5F/I75F, I5F/L144F, I5F/I75F/L144F) were investigated to probe the role of steric bulk within the heme pocket. The mutations significantly increased O(2) association rates (1.5-2.5-fold) and dissociation rates (8-190-fold) as compared to wild-type Tt H-NOX. Structural changes that accompanied the I5F mutation were characterized using X-ray crystallography and resonance Raman spectroscopy. A 1.67 A crystal structure of the I5F mutant indicated that introducing a phenylalanine at position 5 resulted in a significant shift of the N-terminal domain of the protein, causing an opening of the heme pocket. This movement also resulted in an increased amount of flexibility at the N-terminus and the loop covering the N-terminal helix as indicated by the two conformations of the first six N-terminal amino acids, high B-factors in this region of the protein, and partially discontinuous electron density. In addition, introduction of a phenylalanine at position 5 resulted in increased flexibility of the heme within the pocket and weakened hydrogen bonding to the bound O(2) as measured by resonance Raman spectroscopy. This study provides insight into the critical role of I5 in controlling conformational flexibility and ligand affinity in H-NOX proteins.
 
Controlling Conformational Flexibility of an O(2)-Binding H-NOX Domain.,Weinert EE, Phillips-Piro CM, Tran R, Mathies RA, Marletta MA Biochemistry. 2011 Jul 15. PMID:21721586<ref>PMID:21721586</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>


==See Also==
==See Also==
*[[Chemotaxis protein|Chemotaxis protein]]
*[[Chemotaxis protein 3D structures|Chemotaxis protein 3D structures]]
*[[Methyl-accepting chemotaxis protein|Methyl-accepting chemotaxis protein]]
*[[Methyl-accepting chemotaxis protein|Methyl-accepting chemotaxis protein]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Caldanaerobacter subterraneus]]
[[Category: Caldanaerobacter subterraneus subsp. tengcongensis]]
[[Category: Marletta, M A]]
[[Category: Large Structures]]
[[Category: Mathies, R A]]
[[Category: Marletta MA]]
[[Category: Phillips-Piro, C M]]
[[Category: Mathies RA]]
[[Category: Tran, R]]
[[Category: Phillips-Piro CM]]
[[Category: Weinert, E E]]
[[Category: Tran R]]
[[Category: No or o2-sensing protein]]
[[Category: Weinert EE]]
[[Category: Signaling protein]]

Latest revision as of 12:50, 1 March 2024

I5F Mutant Structure of T. Tengcongensis H-NOXI5F Mutant Structure of T. Tengcongensis H-NOX

Structural highlights

3sj5 is a 2 chain structure with sequence from Caldanaerobacter subterraneus subsp. tengcongensis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.673Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q8RBX6_CALS4

See Also

3sj5, resolution 1.67Å

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