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==Crystal structure of Synechococcus sp. PCC 7002 globin at cryogenic temperature with heme modification== | |||
<StructureSection load='4max' size='340' side='right' caption='[[4max]], [[Resolution|resolution]] 1.44Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4max]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Agmenellum_quadruplicatum Agmenellum quadruplicatum]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4i0v 4i0v]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MAX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4MAX FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEB:HEME+B/C'>HEB</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ksc|2ksc]], [[4l2m|4l2m]], [[1rtx|1rtx]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">glbN, SYNPCC7002_A1621 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=32049 Agmenellum quadruplicatum])</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=4max FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4max OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4max RCSB], [http://www.ebi.ac.uk/pdbsum/4max PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The X-ray structures of the hemoglobin from Synechococcus sp. PCC 7002 (GlbN) were solved in the ferric bis-histidine (1.44 A resolution) and cyanide-bound (2.25 A resolution) states with covalently attached heme. The two structures illustrate the conformational changes and cavity opening caused by exogenous ligand binding. They also reveal an unusually distorted heme, ruffled as in c cytochromes. Comparison to the solution structure demonstrates the influence of crystal packing on several structural elements, whereas comparison to GlbN from Synechocystis sp. PCC 6803 shows subtle differences in heme geometries and environment. The new structures will be instrumental in elucidating GlbN reactivity. (c) Proteins 2013;. (c) 2013 Wiley Periodicals, Inc. | |||
The 2/2 hemoglobin from the cyanobacterium Synechococcus sp. PCC 7002 with covalently attached heme: Comparison of X-ray and NMR structures.,Wenke BB, Lecomte JT, Heroux A, Schlessman JL Proteins. 2013 Sep 2. doi: 10.1002/prot.24409. PMID:23999883<ref>PMID:23999883</ref> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Agmenellum quadruplicatum]] | [[Category: Agmenellum quadruplicatum]] | ||
[[Category: Heroux, A | [[Category: Heroux, A]] | ||
[[Category: Lecomte, J T.J | [[Category: Lecomte, J T.J]] | ||
[[Category: Schlessman, J L | [[Category: Schlessman, J L]] | ||
[[Category: Wenke, B B | [[Category: Wenke, B B]] | ||
[[Category: 2/2 globin]] | [[Category: 2/2 globin]] | ||
[[Category: 2/2 hemoglobin]] | [[Category: 2/2 hemoglobin]] | ||
Revision as of 19:48, 21 December 2014
Crystal structure of Synechococcus sp. PCC 7002 globin at cryogenic temperature with heme modificationCrystal structure of Synechococcus sp. PCC 7002 globin at cryogenic temperature with heme modification
Structural highlights
Publication Abstract from PubMedThe X-ray structures of the hemoglobin from Synechococcus sp. PCC 7002 (GlbN) were solved in the ferric bis-histidine (1.44 A resolution) and cyanide-bound (2.25 A resolution) states with covalently attached heme. The two structures illustrate the conformational changes and cavity opening caused by exogenous ligand binding. They also reveal an unusually distorted heme, ruffled as in c cytochromes. Comparison to the solution structure demonstrates the influence of crystal packing on several structural elements, whereas comparison to GlbN from Synechocystis sp. PCC 6803 shows subtle differences in heme geometries and environment. The new structures will be instrumental in elucidating GlbN reactivity. (c) Proteins 2013;. (c) 2013 Wiley Periodicals, Inc. The 2/2 hemoglobin from the cyanobacterium Synechococcus sp. PCC 7002 with covalently attached heme: Comparison of X-ray and NMR structures.,Wenke BB, Lecomte JT, Heroux A, Schlessman JL Proteins. 2013 Sep 2. doi: 10.1002/prot.24409. PMID:23999883[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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