1z6o
From Proteopedia
(New page: 200px<br /><applet load="1z6o" size="450" color="white" frame="true" align="right" spinBox="true" caption="1z6o, resolution 1.91Å" /> '''Crystal Structure of...) |
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| - | [[Image:1z6o.gif|left|200px]]<br /><applet load="1z6o" size=" | + | [[Image:1z6o.gif|left|200px]]<br /><applet load="1z6o" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1z6o, resolution 1.91Å" /> | caption="1z6o, resolution 1.91Å" /> | ||
'''Crystal Structure of Trichoplusia ni secreted ferritin'''<br /> | '''Crystal Structure of Trichoplusia ni secreted ferritin'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Ferritins are iron storage proteins made of 24 subunits forming a hollow | + | Ferritins are iron storage proteins made of 24 subunits forming a hollow spherical shell. Vertebrate ferritins contain varying ratios of heavy (H) and light (L) chains; however, known ferritin structures include only one type of chain and have octahedral symmetry. Here, we report the 1.9A structure of a secreted insect ferritin from Trichoplusia ni, which reveals equal numbers of H and L chains arranged with tetrahedral symmetry. The H/L-chain interface includes complementary features responsible for ordered assembly of the subunits. The H chain contains a ferroxidase active site resembling that of vertebrate H chains with an endogenous, bound iron atom. The L chain lacks the residues that form a putative iron core nucleation site in vertebrate L chains. Instead, a possible nucleation site is observed at the L chain 3-fold pore. The structure also reveals inter- and intrasubunit disulfide bonds, mostly in the extended N-terminal regions unique to insect ferritins. The symmetrical arrangement of H and L chains and the disulfide crosslinks reflect adaptations of insect ferritin to its role as a secreted protein. |
==About this Structure== | ==About this Structure== | ||
| - | 1Z6O is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Trichoplusia_ni Trichoplusia ni] with FE and CA as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1Z6O is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Trichoplusia_ni Trichoplusia ni] with <scene name='pdbligand=FE:'>FE</scene> and <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z6O OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Trichoplusia ni]] | [[Category: Trichoplusia ni]] | ||
| - | [[Category: Bjorkman, P | + | [[Category: Bjorkman, P J.]] |
| - | [[Category: Hamburger, A | + | [[Category: Hamburger, A E.]] |
[[Category: Hamburger, P.]] | [[Category: Hamburger, P.]] | ||
| - | [[Category: Hamburger, Z | + | [[Category: Hamburger, Z A.]] |
| - | [[Category: Jr., A | + | [[Category: Jr., A P.West.]] |
[[Category: CA]] | [[Category: CA]] | ||
[[Category: FE]] | [[Category: FE]] | ||
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[[Category: metal binding protein]] | [[Category: metal binding protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:12:37 2008'' |
Revision as of 14:12, 21 February 2008
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Crystal Structure of Trichoplusia ni secreted ferritin
Overview
Ferritins are iron storage proteins made of 24 subunits forming a hollow spherical shell. Vertebrate ferritins contain varying ratios of heavy (H) and light (L) chains; however, known ferritin structures include only one type of chain and have octahedral symmetry. Here, we report the 1.9A structure of a secreted insect ferritin from Trichoplusia ni, which reveals equal numbers of H and L chains arranged with tetrahedral symmetry. The H/L-chain interface includes complementary features responsible for ordered assembly of the subunits. The H chain contains a ferroxidase active site resembling that of vertebrate H chains with an endogenous, bound iron atom. The L chain lacks the residues that form a putative iron core nucleation site in vertebrate L chains. Instead, a possible nucleation site is observed at the L chain 3-fold pore. The structure also reveals inter- and intrasubunit disulfide bonds, mostly in the extended N-terminal regions unique to insect ferritins. The symmetrical arrangement of H and L chains and the disulfide crosslinks reflect adaptations of insect ferritin to its role as a secreted protein.
About this Structure
1Z6O is a Protein complex structure of sequences from Trichoplusia ni with and as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structure of a secreted insect ferritin reveals a symmetrical arrangement of heavy and light chains., Hamburger AE, West AP Jr, Hamburger ZA, Hamburger P, Bjorkman PJ, J Mol Biol. 2005 Jun 10;349(3):558-69. Epub 2005 Apr 12. PMID:15896348
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