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4a01

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Revision as of 12:59, 25 December 2014

Crystal Structure of the H-Translocating Pyrophosphatase

Structural highlights

4a01 is a 2 chain structure with sequence from Vigna radiata. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , ,
Activity:	Inorganic diphosphatase, with EC number 3.6.1.1
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[O22124_VIGRA] Proton-translocating inorganic pyrophosphatase that contributes to the transtonoplast (from cytosol to vacuole lumen) H(+)-electrochemical potential difference. It establishes a proton gradient of similar and often greater magnitude than the H(+)-ATPase on the same membrane.^[1] ^[2] ^[3] ^[4]

Publication Abstract from PubMed

H(+)-translocating pyrophosphatases (H(+)-PPases) are active proton transporters that establish a proton gradient across the endomembrane by means of pyrophosphate (PP(i)) hydrolysis. H(+)-PPases are found primarily as homodimers in the vacuolar membrane of plants and the plasma membrane of several protozoa and prokaryotes. The three-dimensional structure and detailed mechanisms underlying the enzymatic and proton translocation reactions of H(+)-PPases are unclear. Here we report the crystal structure of a Vigna radiata H(+)-PPase (VrH(+)-PPase) in complex with a non-hydrolysable substrate analogue, imidodiphosphate (IDP), at 2.35 A resolution. Each VrH(+)-PPase subunit consists of an integral membrane domain formed by 16 transmembrane helices. IDP is bound in the cytosolic region of each subunit and trapped by numerous charged residues and five Mg(2+) ions. A previously undescribed proton translocation pathway is formed by six core transmembrane helices. Proton pumping can be initialized by PP(i) hydrolysis, and H(+) is then transported into the vacuolar lumen through a pathway consisting of Arg 242, Asp 294, Lys 742 and Glu 301. We propose a working model of the mechanism for the coupling between proton pumping and PP(i) hydrolysis by H(+)-PPases.

Crystal structure of a membrane-embedded H+-translocating pyrophosphatase.,Lin SM, Tsai JY, Hsiao CD, Huang YT, Chiu CL, Liu MH, Tung JY, Liu TH, Pan RL, Sun YJ Nature. 2012 Mar 28;484(7394):399-403. doi: 10.1038/nature10963. PMID:22456709^[5]

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

References

↑ Yang SJ, Jiang SS, Kuo SY, Hung SH, Tam MF, Pan RL. Localization of a carboxylic residue possibly involved in the inhibition of vacuolar H+-pyrophosphatase by N, N'-dicyclohexylcarbodi-imide. Biochem J. 1999 Sep 15;342 Pt 3:641-6. PMID:10477275
↑ Lin SM, Tsai JY, Hsiao CD, Huang YT, Chiu CL, Liu MH, Tung JY, Liu TH, Pan RL, Sun YJ. Crystal structure of a membrane-embedded H+-translocating pyrophosphatase. Nature. 2012 Mar 28;484(7394):399-403. doi: 10.1038/nature10963. PMID:22456709 doi:10.1038/nature10963
↑ Maeshima M, Yoshida S. Purification and properties of vacuolar membrane proton-translocating inorganic pyrophosphatase from mung bean. J Biol Chem. 1989 Nov 25;264(33):20068-73. PMID:2555340
↑ Nakanishi Y, Maeshima M. Molecular cloning of vacuolar H(+)-pyrophosphatase and its developmental expression in growing hypocotyl of mung bean. Plant Physiol. 1998 Feb;116(2):589-97. PMID:9489011
↑ Lin SM, Tsai JY, Hsiao CD, Huang YT, Chiu CL, Liu MH, Tung JY, Liu TH, Pan RL, Sun YJ. Crystal structure of a membrane-embedded H+-translocating pyrophosphatase. Nature. 2012 Mar 28;484(7394):399-403. doi: 10.1038/nature10963. PMID:22456709 doi:10.1038/nature10963

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/4a01"

@@ Line 7: / Line 7: @@
 <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=4a01 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a01 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4a01 RCSB], [http://www.ebi.ac.uk/pdbsum/4a01 PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/O22124_VIGRA O22124_VIGRA]] Proton-translocating inorganic pyrophosphatase that contributes to the transtonoplast (from cytosol to vacuole lumen) H(+)-electrochemical potential difference. It establishes a proton gradient of similar and often greater magnitude than the H(+)-ATPase on the same membrane.<ref>PMID:10477275</ref> <ref>PMID:22456709</ref> <ref>PMID:2555340</ref> <ref>PMID:9489011</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

4a01

From Proteopedia

Revision as of 12:59, 25 December 2014

Crystal Structure of the H-Translocating Pyrophosphatase

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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