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==Crystal Structure of Synechocystis Hemoglobin with a Covalent Heme Linkage==
==Crystal Structure of Synechocystis Hemoglobin with a Covalent Heme Linkage==
<StructureSection load='1rtx' size='340' side='right' caption='[[1rtx]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='1rtx' size='340' side='right'caption='[[1rtx]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1rtx]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Aphanocapsa_sp._(strain_n-1) Aphanocapsa sp. (strain n-1)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RTX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1RTX FirstGlance]. <br>
<table><tr><td colspan='2'>[[1rtx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechocystis_sp._PCC_6803 Synechocystis sp. PCC 6803]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RTX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RTX FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.8&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GLBN, SLR2097 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1148 Aphanocapsa sp. (strain N-1)])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=1rtx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rtx OCA], [http://pdbe.org/1rtx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1rtx RCSB], [http://www.ebi.ac.uk/pdbsum/1rtx PDBsum]</span></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=1rtx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rtx OCA], [https://pdbe.org/1rtx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rtx RCSB], [https://www.ebi.ac.uk/pdbsum/1rtx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rtx ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/TRHBN_SYNY3 TRHBN_SYNY3]] Forms a very stable complex with oxygen. The oxygen dissociation rate is 0.011 s(-1).  
[https://www.uniprot.org/uniprot/TRHBN_SYNY3 TRHBN_SYNY3] Forms a very stable complex with oxygen. The oxygen dissociation rate is 0.011 s(-1).
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rt/1rtx_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rt/1rtx_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1rtx ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The x-ray crystal structure of Synechocystis hemoglobin has been solved to a resolution of 1.8 A. The conformation of this structure is surprisingly different from that of the previously reported solution structure, probably due in part to a covalent linkage between the heme 2-vinyl and His117 that is present in the crystal structure but not in the structure solved by NMR. Synechocystis hemoglobin is a hexacoordinate hemoglobin in which the heme iron is coordinated by both the proximal and distal histidines. It is also a member of the "truncated hemoglobin" family that is much shorter in primary structure than vertebrate and plant hemoglobins. In contrast to other truncated hemoglobins, the crystal structure of Synechocystis hemoglobin displays no "ligand tunnel" and shows that several important amino acid side chains extrude into the solvent instead of residing inside the heme pocket. The stereochemistry of hexacoordination is compared with other hexacoordinate hemoglobins and cytochromes in an effort to illuminate factors contributing to ligand affinity in hexacoordinate hemoglobins.
The crystal structure of Synechocystis hemoglobin with a covalent heme linkage.,Hoy JA, Kundu S, Trent JT 3rd, Ramaswamy S, Hargrove MS J Biol Chem. 2004 Apr 16;279(16):16535-42. Epub 2004 Jan 21. PMID:14736872<ref>PMID:14736872</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1rtx" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Hemoglobin 3D structures|Hemoglobin 3D structures]]
*[[Hemoglobin 3D structures|Hemoglobin 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Hargrove, M S]]
[[Category: Large Structures]]
[[Category: Hoy, J A]]
[[Category: Synechocystis sp. PCC 6803]]
[[Category: Kundu, S]]
[[Category: Hargrove MS]]
[[Category: Ramaswamy, S]]
[[Category: Hoy JA]]
[[Category: Trent, J T]]
[[Category: Kundu S]]
[[Category: Hemichrome]]
[[Category: Ramaswamy S]]
[[Category: Hexacoordinate]]
[[Category: Trent JT]]
[[Category: Oxygen storage-transport complex]]
[[Category: Synechocystis hemoglobin]]
[[Category: Truncated]]

Latest revision as of 11:26, 14 February 2024

Crystal Structure of Synechocystis Hemoglobin with a Covalent Heme LinkageCrystal Structure of Synechocystis Hemoglobin with a Covalent Heme Linkage

Structural highlights

1rtx is a 1 chain structure with sequence from Synechocystis sp. PCC 6803. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.8Å
Ligands:, , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

TRHBN_SYNY3 Forms a very stable complex with oxygen. The oxygen dissociation rate is 0.011 s(-1).

Evolutionary Conservation

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

See Also

1rtx, resolution 1.80Å

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