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==Crystal structure of cytochrome c6 Q57V mutant from Synechococcus sp. PCC 7002==
==Crystal structure of cytochrome c6 Q57V mutant from Synechococcus sp. PCC 7002==
<StructureSection load='4eid' size='340' side='right' caption='[[4eid]], [[Resolution|resolution]] 1.13&Aring;' scene=''>
<StructureSection load='4eid' size='340' side='right'caption='[[4eid]], [[Resolution|resolution]] 1.13&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4eid]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Agmenellum_quadruplicatum Agmenellum quadruplicatum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EID OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EID FirstGlance]. <br>
<table><tr><td colspan='2'>[[4eid]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Agmenellum_quadruplicatum Agmenellum quadruplicatum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EID OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EID 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>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3dr0|3dr0]], [[4eic|4eic]], [[4eie|4eie]], [[4eif|4eif]]</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3dr0|3dr0]], [[4eic|4eic]], [[4eie|4eie]], [[4eif|4eif]]</div></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">petJ, petJ1, SYNPCC7002_A0167 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=32049 Agmenellum quadruplicatum])</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">petJ, petJ1, SYNPCC7002_A0167 ([https://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=4eid FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eid OCA], [http://pdbe.org/4eid PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4eid RCSB], [http://www.ebi.ac.uk/pdbsum/4eid PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4eid ProSAT]</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=4eid FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eid OCA], [https://pdbe.org/4eid PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4eid RCSB], [https://www.ebi.ac.uk/pdbsum/4eid PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4eid ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/CYC6_SYNP2 CYC6_SYNP2]] Functions as an electron carrier between membrane-bound cytochrome b6-f and photosystem I in oxygenic photosynthesis (By similarity).  
[[https://www.uniprot.org/uniprot/CYC6_SYNP2 CYC6_SYNP2]] Functions as an electron carrier between membrane-bound cytochrome b6-f and photosystem I in oxygenic photosynthesis (By similarity).  
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 4eid" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 4eid" style="background-color:#fffaf0;"></div>
==See Also==
*[[Cytochrome C 3D structures|Cytochrome C 3D structures]]
*[[Cytochrome f 3D structures|Cytochrome f 3D structures]]
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Agmenellum quadruplicatum]]
[[Category: Agmenellum quadruplicatum]]
[[Category: Large Structures]]
[[Category: Bialek, W]]
[[Category: Bialek, W]]
[[Category: Jaskolski, M]]
[[Category: Jaskolski, M]]

Revision as of 20:27, 10 March 2021

Crystal structure of cytochrome c6 Q57V mutant from Synechococcus sp. PCC 7002Crystal structure of cytochrome c6 Q57V mutant from Synechococcus sp. PCC 7002

Structural highlights

4eid is a 1 chain structure with sequence from Agmenellum quadruplicatum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:,
Gene:petJ, petJ1, SYNPCC7002_A0167 (Agmenellum quadruplicatum)
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[CYC6_SYNP2] Functions as an electron carrier between membrane-bound cytochrome b6-f and photosystem I in oxygenic photosynthesis (By similarity).

Publication Abstract from PubMed

The structure of the reduced form of cytochrome c(6) from the mesophilic cyanobacterium Synechococcus sp. PCC 7002 has been determined at 1.2 A and refined to an R-factor of 0.107. This protein is unique among all known cytochromes c(6), owing to the presence of an unusual seven-residue insertion, KDGSKSL(44-50), which differs from the insertion found in the recently discovered plant cytochromes c(6A). Furthermore, the present protein is unusual because of its very high content (36%) of the smallest residues (glycine and alanine). The structure reveals that the overall fold of the protein is similar to that of other class I c-type cytochromes, despite the presence of the specific insertion. The insertion is located within the most variable region of the cytochrome c(6) sequence, i.e. between helices II and III. The first six residues [KDGSKS(44-49)] form a loop, whereas the last residue, Leu50, extends the N-terminal beginning of helix III. Several specific noncovalent interactions are found inside the insertion, as well as between the insertion and the rest of the protein. The crystal structure contains three copies of the cytochrome c(6) molecule per asymmetric unit, and is characterized by an unusually high packing density, with solvent occupying barely 17.58% of the crystal volume.

Atomic-resolution structure of reduced cyanobacterial cytochrome c6 with an unusual sequence insertion.,Bialek W, Krzywda S, Jaskolski M, Szczepaniak A FEBS J. 2009 Aug;276(16):4426-36. PMID:19678839[1]

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

See Also

References

  1. Bialek W, Krzywda S, Jaskolski M, Szczepaniak A. Atomic-resolution structure of reduced cyanobacterial cytochrome c6 with an unusual sequence insertion. FEBS J. 2009 Aug;276(16):4426-36. PMID:19678839 doi:10.1111/j.1742-4658.2009.07150.x

4eid, resolution 1.13Å

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