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[[Image:1rtx.jpg|left|200px]]<br /><applet load="1rtx" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1rtx, resolution 1.80&Aring;" />
'''Crystal Structure of Synechocystis Hemoglobin with a Covalent Heme Linkage'''<br />


==Overview==
==Crystal Structure of Synechocystis Hemoglobin with a Covalent Heme Linkage==
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.
<StructureSection load='1rtx' size='340' side='right'caption='[[1rtx]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<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='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='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'>[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>
== Function ==
[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 ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <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>
    <text>to colour the structure by Evolutionary Conservation</text>
  </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/main_output.php?pdb_ID=1rtx ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1RTX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Synechocystis_sp. Synechocystis sp.] with <scene name='pdbligand=CD:'>CD</scene>, <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=K:'>K</scene> and <scene name='pdbligand=HEM:'>HEM</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RTX OCA].
*[[Hemoglobin 3D structures|Hemoglobin 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14736872 14736872]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Synechocystis sp. PCC 6803]]
[[Category: Synechocystis sp.]]
[[Category: Hargrove MS]]
[[Category: Hargrove, M.S.]]
[[Category: Hoy JA]]
[[Category: Hoy, J.A.]]
[[Category: Kundu S]]
[[Category: Kundu, S.]]
[[Category: Ramaswamy S]]
[[Category: Ramaswamy, S.]]
[[Category: Trent JT]]
[[Category: Trent, J.T.]]
[[Category: CD]]
[[Category: HEM]]
[[Category: K]]
[[Category: SO4]]
[[Category: crystal structure]]
[[Category: hemichrome]]
[[Category: hexacoordinate]]
[[Category: synechocystis hemoglobin]]
[[Category: truncated]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:50:08 2008''

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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