5lbd

From Proteopedia

(Difference between revisions)

Revision as of 07:05, 5 August 2020

Crystal structure of the N-domain of HMA6, a copper-transporting P-type ATPase

Structural highlights

5lbd is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , ,
NonStd Res:
Activity:	Cu(+) exporting ATPase, with EC number 3.6.3.54
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[HMA6_ARATH] Mediates copper transfer across the plastid envelope. Required for the delivery of copper into the plastid stroma, which is essential for the function of copper proteins. Seems to be selective for monovalent copper Cu(+) transport. Plays also a role in glucose signaling-mediated cell proliferation of root meristem in non-green tissues.^[1] ^[2] ^[3] ^[4]

Publication Abstract from PubMed

Copper is a crucial ion in cells, but needs to be closely controlled due to its toxic potential and ability to catalyse the formation of radicals. In chloroplasts, an important step for the proper functioning of the photosynthetic electron transfer chain is the delivery of copper to plastocyanin in the thylakoid lumen. The main route for copper transport to the thylakoid lumen is driven by two PIB-type ATPases, Heavy Metal ATPase 6 (HMA6) and HMA8, located in the inner membrane of the chloroplast envelope and in the thylakoid membrane, respectively. Here, the crystal structures of the nucleotide binding domain of HMA6 and HMA8 from Arabidopsis thaliana are reported at 1.5A and 1.75A resolution, respectively, providing the first structural information on plants Cu+-ATPases. The structures reveal a compact domain, with two short helices on both sides of a twisted beta-sheet. A double mutant, aiding in the crystallization, provides a new crystal contact, but also avoids an internal clash highlighting the benefits of construct modifications. Finally, the histidine in the HP motif of the isolated domains, unable to bind ATP, shows a side chain conformation distinct from nucleotide bound structures.

Structural Insights into the Nucleotide-Binding Domains of the P1B-type ATPases HMA6 and HMA8 from Arabidopsis thaliana.,Mayerhofer H, Sautron E, Rolland N, Catty P, Seigneurin-Berny D, Pebay-Peyroula E, Ravaud S PLoS One. 2016 Nov 1;11(11):e0165666. doi: 10.1371/journal.pone.0165666., eCollection 2016. PMID:27802305^[5]

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

References

↑ Shikanai T, Muller-Moule P, Munekage Y, Niyogi KK, Pilon M. PAA1, a P-type ATPase of Arabidopsis, functions in copper transport in chloroplasts. Plant Cell. 2003 Jun;15(6):1333-46. PMID:12782727
↑ Abdel-Ghany SE, Muller-Moule P, Niyogi KK, Pilon M, Shikanai T. Two P-type ATPases are required for copper delivery in Arabidopsis thaliana chloroplasts. Plant Cell. 2005 Apr;17(4):1233-51. Epub 2005 Mar 16. PMID:15772282 doi:http://dx.doi.org/10.1105/tpc.104.030452
↑ Catty P, Boutigny S, Miras R, Joyard J, Rolland N, Seigneurin-Berny D. Biochemical characterization of AtHMA6/PAA1, a chloroplast envelope Cu(I)-ATPase. J Biol Chem. 2011 Oct 21;286(42):36188-97. doi: 10.1074/jbc.M111.241034. Epub, 2011 Aug 30. PMID:21878617 doi:http://dx.doi.org/10.1074/jbc.M111.241034
↑ Yamada K, Lim J, Dale JM, Chen H, Shinn P, Palm CJ, Southwick AM, Wu HC, Kim C, Nguyen M, Pham P, Cheuk R, Karlin-Newmann G, Liu SX, Lam B, Sakano H, Wu T, Yu G, Miranda M, Quach HL, Tripp M, Chang CH, Lee JM, Toriumi M, Chan MM, Tang CC, Onodera CS, Deng JM, Akiyama K, Ansari Y, Arakawa T, Banh J, Banno F, Bowser L, Brooks S, Carninci P, Chao Q, Choy N, Enju A, Goldsmith AD, Gurjal M, Hansen NF, Hayashizaki Y, Johnson-Hopson C, Hsuan VW, Iida K, Karnes M, Khan S, Koesema E, Ishida J, Jiang PX, Jones T, Kawai J, Kamiya A, Meyers C, Nakajima M, Narusaka M, Seki M, Sakurai T, Satou M, Tamse R, Vaysberg M, Wallender EK, Wong C, Yamamura Y, Yuan S, Shinozaki K, Davis RW, Theologis A, Ecker JR. Empirical analysis of transcriptional activity in the Arabidopsis genome. Science. 2003 Oct 31;302(5646):842-6. PMID:14593172 doi:http://dx.doi.org/10.1126/science.1088305
↑ Mayerhofer H, Sautron E, Rolland N, Catty P, Seigneurin-Berny D, Pebay-Peyroula E, Ravaud S. Structural Insights into the Nucleotide-Binding Domains of the P1B-type ATPases HMA6 and HMA8 from Arabidopsis thaliana. PLoS One. 2016 Nov 1;11(11):e0165666. doi: 10.1371/journal.pone.0165666., eCollection 2016. PMID:27802305 doi:http://dx.doi.org/10.1371/journal.pone.0165666

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 1: / Line 1: @@
 ==Crystal structure of the N-domain of HMA6, a copper-transporting P-type ATPase==
-<StructureSection load='5lbd' size='340' side='right' caption='[[5lbd]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
+<StructureSection load='5lbd' size='340' side='right'caption='[[5lbd]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5lbd]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LBD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LBD FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5lbd]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LBD OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5LBD FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=NH4:AMMONIUM+ION'>NH4</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=NH4:AMMONIUM+ION'>NH4</scene></td></tr>
 <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cu(+)_exporting_ATPase Cu(+) exporting ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.54 3.6.3.54] </span></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=5lbd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lbd OCA], [http://pdbe.org/5lbd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lbd RCSB], [http://www.ebi.ac.uk/pdbsum/5lbd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lbd ProSAT]</span></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=5lbd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lbd OCA], [http://pdbe.org/5lbd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lbd RCSB], [http://www.ebi.ac.uk/pdbsum/5lbd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lbd ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 20: / Line 20: @@
 </div>
 <div class="pdbe-citations 5lbd" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[ATPase 3D structures|ATPase 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
+[[Category: Large Structures]]
 [[Category: Mayerhofer, H]]
 [[Category: Pebay-Peyroula, E]]

5lbd

From Proteopedia

Revision as of 07:05, 5 August 2020

Crystal structure of the N-domain of HMA6, a copper-transporting P-type ATPase

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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