1u55

From Proteopedia

(Difference between revisions)

Current revision

Crystal structure of an oxygen binding H-NOX domain related to soluble guanylate cyclases (oxygen complex)

Structural highlights

1u55 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 1.77Å
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q8RBX6_CALS4

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Soluble guanylate cyclases are nitric oxide-responsive signaling proteins in which the nitric oxide sensor is a heme-binding domain of unknown structure that we have termed the heme-NO and oxygen binding (H-NOX) domain. H-NOX domains are also found in bacteria, either as isolated domains, or are fused through a membrane-spanning region to methyl-accepting chemotaxis proteins. We have determined the crystal structure of an oxygen-binding H-NOX domain of one such signaling protein from the obligate anaerobe Thermoanaerobacter tengcongensis at 1.77-angstroms resolution, revealing a protein fold unrelated to known structures. Particularly striking is the structure of the protoporphyrin IX group, which is distorted from planarity to an extent not seen before in protein-bound heme groups. Comparison of the structure of the H-NOX domain in two different crystal forms suggests a mechanism whereby alteration in the degree of distortion of the heme group is coupled to changes on the molecular surface of the H-NOX domain and potentially to changes in intermolecular interactions.

Crystal structure of an oxygen-binding heme domain related to soluble guanylate cyclases.,Pellicena P, Karow DS, Boon EM, Marletta MA, Kuriyan J Proc Natl Acad Sci U S A. 2004 Aug 31;101(35):12854-9. Epub 2004 Aug 23. PMID:15326296^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Pellicena P, Karow DS, Boon EM, Marletta MA, Kuriyan J. Crystal structure of an oxygen-binding heme domain related to soluble guanylate cyclases. Proc Natl Acad Sci U S A. 2004 Aug 31;101(35):12854-9. Epub 2004 Aug 23. PMID:15326296 doi:10.1073/pnas.0405188101

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1u55"

@@ Line 1: / Line 1: @@
 ==Crystal structure of an oxygen binding H-NOX domain related to soluble guanylate cyclases (oxygen complex)==
-<StructureSection load='1u55' size='340' side='right' caption='[[1u55]], [[Resolution|resolution]] 1.77&Aring;' scene=''>
+<StructureSection load='1u55' size='340' side='right'caption='[[1u55]], [[Resolution|resolution]] 1.77&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1u55]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/As_1.2430 As 1.2430]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U55 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1U55 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1u55]] 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=1U55 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1U55 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</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]] 1.77&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1u4h|1u4h]], [[1u56|1u56]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Tar4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=119072 AS 1.2430])</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=1u55 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u55 OCA], [https://pdbe.org/1u55 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1u55 RCSB], [https://www.ebi.ac.uk/pdbsum/1u55 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1u55 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=1u55 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u55 OCA], [http://pdbe.org/1u55 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1u55 RCSB], [http://www.ebi.ac.uk/pdbsum/1u55 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1u55 ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/Q8RBX6_CALS4 Q8RBX6_CALS4]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 30: / Line 31: @@
 ==See Also==
-*[[Chemotaxis protein|Chemotaxis protein]]
+*[[Chemotaxis protein 3D structures|Chemotaxis protein 3D structures]]
 *[[Methyl-accepting chemotaxis protein|Methyl-accepting chemotaxis protein]]
 == References ==
@@ Line 36: / Line 37: @@
 __TOC__
 </StructureSection>
-[[Category: As 1 2430]]
+[[Category: Caldanaerobacter subterraneus subsp. tengcongensis]]
-[[Category: Boon, E M]]
+[[Category: Large Structures]]
-[[Category: Karow, D S]]
+[[Category: Boon EM]]
-[[Category: Kuriyan, J]]
+[[Category: Karow DS]]
-[[Category: Marletta, M A]]
+[[Category: Kuriyan J]]
-[[Category: Pellicena, P]]
+[[Category: Marletta MA]]
-[[Category: Chemotaxis]]
+[[Category: Pellicena P]]
-[[Category: H-nox domain]]
-[[Category: Heme]]
-[[Category: Oxygen sensor]]
-[[Category: Signal transduction]]
-[[Category: Signaling protein]]

1u55

From Proteopedia

Current revision

Crystal structure of an oxygen binding H-NOX domain related to soluble guanylate cyclases (oxygen complex)

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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