3hhs

From Proteopedia

(Difference between revisions)

Revision as of 20:49, 24 December 2014

Crystal Structure of Manduca sexta prophenoloxidase

Structural highlights

3hhs is a 2 chain structure with sequence from Manduca sexta. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Activity:	Monophenol monooxygenase, with EC number 1.14.18.1
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[PRP2_MANSE] This is a copper-containing oxidase that functions in the formation of pigments such as melanins and other polyphenolic compounds. Catalyzes the rate-limiting conversions of tyrosine to DOPA, DOPA to DOPA-quinone and possibly 5,6 dihydroxyindole to indole-5'6 quinone. Binds to the surface of hemocytes and is involved in hemocyte melanization.^[1] [PRP1_MANSE] This is a copper-containing oxidase that functions in the formation of pigments such as melanins and other polyphenolic compounds. Catalyzes the rate-limiting conversions of tyrosine to DOPA, DOPA to DOPA-quinone and possibly 5,6 dihydroxyindole to indole-5'6 quinone. Binds to the surface of hemocytes and is involved in hemocyte melanization.^[2] ^[3]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Arthropod phenoloxidase (PO) generates quinones and other toxic compounds to sequester and kill pathogens during innate immune responses. It is also involved in wound healing and other physiological processes. Insect PO is activated from its inactive precursor, prophenoloxidase (PPO), by specific proteolysis via a serine protease cascade. Here, we report the crystal structure of PPO from a lepidopteran insect at a resolution of 1.97 A, which is the initial structure for a PPO from the type 3 copper protein family. Manduca sexta PPO is a heterodimer consisting of 2 homologous polypeptide chains, PPO1 and PPO2. The active site of each subunit contains a canonical type 3 di-nuclear copper center, with each copper ion coordinated with 3 structurally conserved histidines. The acidic residue Glu-395 located at the active site of PPO2 may serve as a general base for deprotonation of monophenolic substrates, which is key to the ortho-hydroxylase activity of PO. The structure provides unique insights into the mechanism by which type 3 copper proteins differ in their enzymatic activities, albeit sharing a common active center. A drastic change in electrostatic surface induced on cleavage at Arg-51 allows us to propose a model for localized PPO activation in insects.

Crystal structure of Manduca sexta prophenoloxidase provides insights into the mechanism of type 3 copper enzymes.,Li Y, Wang Y, Jiang H, Deng J Proc Natl Acad Sci U S A. 2009 Oct 6;106(40):17002-6. Epub 2009 Sep 28. PMID:19805072^[4]

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

References

↑ Ling E, Yu XQ. Prophenoloxidase binds to the surface of hemocytes and is involved in hemocyte melanization in Manduca sexta. Insect Biochem Mol Biol. 2005 Dec;35(12):1356-66. Epub 2005 Sep 21. PMID:16291091 doi:http://dx.doi.org/S0965-1748(05)00172-4
↑ Ling E, Yu XQ. Prophenoloxidase binds to the surface of hemocytes and is involved in hemocyte melanization in Manduca sexta. Insect Biochem Mol Biol. 2005 Dec;35(12):1356-66. Epub 2005 Sep 21. PMID:16291091 doi:http://dx.doi.org/S0965-1748(05)00172-4
↑ Jiang H, Wang Y, Ma C, Kanost MR. Subunit composition of pro-phenol oxidase from Manduca sexta: molecular cloning of subunit ProPO-P1. Insect Biochem Mol Biol. 1997 Oct;27(10):835-50. PMID:9474780
↑ Li Y, Wang Y, Jiang H, Deng J. Crystal structure of Manduca sexta prophenoloxidase provides insights into the mechanism of type 3 copper enzymes. Proc Natl Acad Sci U S A. 2009 Oct 6;106(40):17002-6. Epub 2009 Sep 28. PMID:19805072

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3hhs"

@@ 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=3hhs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hhs OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3hhs RCSB], [http://www.ebi.ac.uk/pdbsum/3hhs PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/PRP2_MANSE PRP2_MANSE]] This is a copper-containing oxidase that functions in the formation of pigments such as melanins and other polyphenolic compounds. Catalyzes the rate-limiting conversions of tyrosine to DOPA, DOPA to DOPA-quinone and possibly 5,6 dihydroxyindole to indole-5'6 quinone. Binds to the surface of hemocytes and is involved in hemocyte melanization.<ref>PMID:16291091</ref>  [[http://www.uniprot.org/uniprot/PRP1_MANSE PRP1_MANSE]] This is a copper-containing oxidase that functions in the formation of pigments such as melanins and other polyphenolic compounds. Catalyzes the rate-limiting conversions of tyrosine to DOPA, DOPA to DOPA-quinone and possibly 5,6 dihydroxyindole to indole-5'6 quinone. Binds to the surface of hemocytes and is involved in hemocyte melanization.<ref>PMID:16291091</ref> <ref>PMID:9474780</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

3hhs

From Proteopedia

Revision as of 20:49, 24 December 2014

Crystal Structure of Manduca sexta prophenoloxidase

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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