5had

From Proteopedia

(Difference between revisions)

Revision as of 07:28, 9 August 2023

Crystal structure of intermembrane space region of chloroplast protein ARC6

Structural highlights

5had is a 1 chain structure with sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.238Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.^[1] ^[2] ^[3] ^[4] ^[5] ^[6] ^[7] ^[8]

Publication Abstract from PubMed

Chloroplasts divide by binary fission, which is accomplished by the simultaneous constriction of the FtsZ ring on the stromal side of the inner envelope membrane, and the ARC5 ring on the cytosolic side of the outer envelope membrane. The two rings are connected and coordinated mainly by the interaction between the inner envelope membrane protein ARC6 and the outer envelope membrane protein PDV2 in the intermembrane space. The underlying mechanism of this coordination is unclear to date. Here, we solved the crystal structure of the intermembrane space region of the ARC6-PDV2 complex. The results indicated that PDV2 inserts its carboxy terminus into a pocket formed in ARC6, and this interaction further induces the dimerization of the intermembrane space regions of two ARC6 molecules. A pdv2 mutant attenuating PDV2-induced ARC6 dimerization showed abnormal morphology of ARC6 rings and compromised chloroplast division in plant cells. Together, our data reveal that PDV2-induced dimerization of ARC6 plays a critical role in chloroplast division and provide insights into the coordination mechanism of the internal and external plastid division machineries.

Structural insights into the coordination of plastid division by the ARC6-PDV2 complex.,Wang W, Li J, Sun Q, Yu X, Zhang W, Jia N, An C, Li Y, Dong Y, Han F, Chang N, Liu X, Zhu Z, Yu Y, Fan S, Yang M, Luo SZ, Gao H, Feng Y Nat Plants. 2017 Mar 1;3:17011. doi: 10.1038/nplants.2017.11. PMID:28248291^[9]

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

References

↑ Marrison JL, Rutherford SM, Robertson EJ, Lister C, Dean C, Leech RM. The distinctive roles of five different ARC genes in the chloroplast division process in Arabidopsis. Plant J. 1999 Jun;18(6):651-62. PMID:10417716
↑ Yamamoto K, Pyke KA, Kiss JZ. Reduced gravitropism in inflorescence stems and hypocotyls, but not roots, of Arabidopsis mutants with large plastids. Physiol Plant. 2002 Apr;114(4):627-636. PMID:11975738
↑ Pyke KA, Rutherford SM, Robertson EJ, Leech RM. arc6, A Fertile Arabidopsis Mutant with Only Two Mesophyll Cell Chloroplasts. Plant Physiol. 1994 Nov;106(3):1169-1177. PMID:12232400
↑ Vitha S, Froehlich JE, Koksharova O, Pyke KA, van Erp H, Osteryoung KW. ARC6 is a J-domain plastid division protein and an evolutionary descendant of the cyanobacterial cell division protein Ftn2. Plant Cell. 2003 Aug;15(8):1918-33. PMID:12897262
↑ Holzinger A, Kwok EY, Hanson MR. Effects of arc3, arc5 and arc6 mutations on plastid morphology and stromule formation in green and nongreen tissues of Arabidopsis thaliana. Photochem Photobiol. 2008 Nov-Dec;84(6):1324-35. doi:, 10.1111/j.1751-1097.2008.00437.x. Epub 2008 Aug 29. PMID:18764889 doi:http://dx.doi.org/10.1111/j.1751-1097.2008.00437.x
↑ Glynn JM, Froehlich JE, Osteryoung KW. Arabidopsis ARC6 coordinates the division machineries of the inner and outer chloroplast membranes through interaction with PDV2 in the intermembrane space. Plant Cell. 2008 Sep;20(9):2460-70. doi: 10.1105/tpc.108.061440. Epub 2008 Sep, 23. PMID:18812496 doi:http://dx.doi.org/10.1105/tpc.108.061440
↑ Robertson EJ, Pyke KA, Leech RM. arc6, an extreme chloroplast division mutant of Arabidopsis also alters proplastid proliferation and morphology in shoot and root apices. J Cell Sci. 1995 Sep;108 ( Pt 9):2937-44. PMID:8537433
↑ Pyke KA, Page AM. Plastid ontogeny during petal development in Arabidopsis. Plant Physiol. 1998 Feb;116(2):797-803. PMID:9489024
↑ Wang W, Li J, Sun Q, Yu X, Zhang W, Jia N, An C, Li Y, Dong Y, Han F, Chang N, Liu X, Zhu Z, Yu Y, Fan S, Yang M, Luo SZ, Gao H, Feng Y. Structural insights into the coordination of plastid division by the ARC6-PDV2 complex. Nat Plants. 2017 Mar 1;3:17011. doi: 10.1038/nplants.2017.11. PMID:28248291 doi:http://dx.doi.org/10.1038/nplants.2017.11

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5had"

Categories: Arabidopsis thaliana | Large Structures | Feng Y | Yu X

@@ Line 3: / Line 3: @@
 <StructureSection load='5had' size='340' side='right'caption='[[5had]], [[Resolution|resolution]] 2.24&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5had]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HAD OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5HAD FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5had]] 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=5HAD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5HAD FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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]] 2.238&#8491;</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5had FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5had OCA], [http://pdbe.org/5had PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5had RCSB], [http://www.ebi.ac.uk/pdbsum/5had PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5had ProSAT]</span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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=5had FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5had OCA], [https://pdbe.org/5had PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5had RCSB], [https://www.ebi.ac.uk/pdbsum/5had PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5had ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://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 ==
@@ Line 22: / Line 23: @@
 __TOC__
 </StructureSection>
+[[Category: Arabidopsis thaliana]]
 [[Category: Large Structures]]
-[[Category: Feng, Y]]
+[[Category: Feng Y]]
-[[Category: Yu, X]]
+[[Category: Yu X]]
-[[Category: Chloroplast]]
-[[Category: Intermembrane space]]
-[[Category: Photosynthesis]]

5had

From Proteopedia

Revision as of 07:28, 9 August 2023

Crystal structure of intermembrane space region of chloroplast protein ARC6

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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