5d9r
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5d9r]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5D9R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5D9R FirstGlance]. <br> | <table><tr><td colspan='2'>[[5d9r]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5D9R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5D9R FirstGlance]. <br> | ||
| - | </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=5d9r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d9r OCA], [https://pdbe.org/5d9r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5d9r RCSB], [https://www.ebi.ac.uk/pdbsum/5d9r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5d9r ProSAT]</span></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]] 2.052Å</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=5d9r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d9r OCA], [https://pdbe.org/5d9r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5d9r RCSB], [https://www.ebi.ac.uk/pdbsum/5d9r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5d9r ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/ARC6_ARATH ARC6_ARATH] Component of the plastid division machinery. Involved in the initiation of proplastid and plastid division (including chloroplasts, statoliths and leukoplasts). Promotes the assembly and/or stabilization of the plastid-dividing FtsZ ring, functioning as an antagonistic regulator of FtsZ dynamics against CDP1. Relays plastid division site position between stroma and outer surface via interactions with the stromal FtsZ ring and the outer membrane PDV2 that recruits cytoplasmic ARC5 ring. Required for plastid equatorial positioning of PDV2 and ARC5. May contribute to gravitropism in stems and hypocotyls. Seems to influence stromule (stroma-filled tubular extensions of the plastid envelope membrane) length and frequency.<ref>PMID:10417716</ref> <ref>PMID:11975738</ref> <ref>PMID:12232400</ref> <ref>PMID:12897262</ref> <ref>PMID:18764889</ref> <ref>PMID:18812496</ref> <ref>PMID:8537433</ref> <ref>PMID:9489024</ref> | [https://www.uniprot.org/uniprot/ARC6_ARATH ARC6_ARATH] Component of the plastid division machinery. Involved in the initiation of proplastid and plastid division (including chloroplasts, statoliths and leukoplasts). Promotes the assembly and/or stabilization of the plastid-dividing FtsZ ring, functioning as an antagonistic regulator of FtsZ dynamics against CDP1. Relays plastid division site position between stroma and outer surface via interactions with the stromal FtsZ ring and the outer membrane PDV2 that recruits cytoplasmic ARC5 ring. Required for plastid equatorial positioning of PDV2 and ARC5. May contribute to gravitropism in stems and hypocotyls. Seems to influence stromule (stroma-filled tubular extensions of the plastid envelope membrane) length and frequency.<ref>PMID:10417716</ref> <ref>PMID:11975738</ref> <ref>PMID:12232400</ref> <ref>PMID:12897262</ref> <ref>PMID:18764889</ref> <ref>PMID:18812496</ref> <ref>PMID:8537433</ref> <ref>PMID:9489024</ref> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The chloroplast division machinery is composed of numerous proteins that assemble as a large complex to divide double-membraned chloroplasts through binary fission. A key mediator of division-complex formation is ARC6, a chloroplast inner envelope protein and evolutionary descendant of the cyanobacterial cell division protein Ftn2. ARC6 connects stromal and cytosolic contractile rings across the two membranes through interaction with an outer envelope protein within the intermembrane space (IMS). The ARC6 IMS region bears a structurally uncharacterized domain of unknown function, DUF4101, that is highly conserved among ARC6 and Ftn2 proteins. Here we report the crystal structure of this domain from Arabidopsis thaliana ARC6. The domain forms an alpha/beta barrel open towards the outer envelope membrane but closed towards the inner envelope membrane. These findings provide new clues into how ARC6 and its homologs contribute to chloroplast and cyanobacterial cell division. | ||
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| - | Crystal structure of a conserved domain in the intermembrane space region of the plastid division protein ARC6.,Kumar N, Radhakrishnan A, Su CC, Osteryoung KW, Yu EW Protein Sci. 2016 Feb;25(2):523-9. doi: 10.1002/pro.2825. Epub 2015 Oct 29. PMID:26452626<ref>PMID:26452626</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 5d9r" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Current revision
Crystal structure of a conserved domain in the intermembrane space region of the plastid division protein ARC6
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