1aew: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1aew.gif|left|200px]]<br /><applet load="1aew" size=" | [[Image:1aew.gif|left|200px]]<br /><applet load="1aew" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1aew, resolution 1.95Å" /> | caption="1aew, resolution 1.95Å" /> | ||
'''L-CHAIN HORSE APOFERRITIN'''<br /> | '''L-CHAIN HORSE APOFERRITIN'''<br /> | ||
| Line 7: | Line 7: | ||
==About this Structure== | ==About this Structure== | ||
1AEW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus] with CD as [http://en.wikipedia.org/wiki/ligand ligand]. The following page contains interesting information on the relation of 1AEW with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb35_1.html Ferritin and Transferrin]]. Known structural/functional Sites: <scene name='pdbsite=NCL:Putative Fe Core Nucleation Site In Ferritins'>NCL</scene>, <scene name='pdbsite=SS1:Intermolecular Crystal Contact. This Cd Bridge Links 2 S ...'>SS1</scene>, <scene name='pdbsite=SS2:These Cd Atoms Are Observed On Or Near The Crystallograp ...'>SS2</scene> and <scene name='pdbsite=SS3:Metal Binding Site On The Inner Surface Of Protein Shell ...'>SS3</scene>. Full crystallographic information is available from [http:// | 1AEW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus] with <scene name='pdbligand=CD:'>CD</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. The following page contains interesting information on the relation of 1AEW with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb35_1.html Ferritin and Transferrin]]. Known structural/functional Sites: <scene name='pdbsite=NCL:Putative+Fe+Core+Nucleation+Site+In+Ferritins'>NCL</scene>, <scene name='pdbsite=SS1:Intermolecular+Crystal+Contact.+This+Cd+Bridge+Links+2+S+...'>SS1</scene>, <scene name='pdbsite=SS2:These+Cd+Atoms+Are+Observed+On+Or+Near+The+Crystallograp+...'>SS2</scene> and <scene name='pdbsite=SS3:Metal+Binding+Site+On+The+Inner+Surface+Of+Protein+Shell+...'>SS3</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AEW OCA]. | ||
==Reference== | ==Reference== | ||
| Line 24: | Line 24: | ||
[[Category: multigene family]] | [[Category: multigene family]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:30:06 2008'' | ||
Revision as of 10:30, 3 February 2008
|
L-CHAIN HORSE APOFERRITIN
OverviewOverview
Mammalian ferritins are 24-mers assembled from two types of polypeptide, chain which provide the molecule with different functions. H(eavy) chains, catalyse the first step in iron storage, the oxidation of iron(II)., L(ight) chains promote the nucleation of the mineral ferrihydrite enabling, storage of iron(III) inside the protein shell. We report here the, comparison of the three-dimensional structures of recombinant human H, chain (HuHF) and horse L chain (HoLF) ferritin homopolymers, which have, been refined at 1.9 A resolution. There is 53% sequence identity between, these molecules, and the two structures are very similar, the H and L, subunit alpha-carbons superposing to within 0.5 A rms deviation with 41, water molecules in common. Nevertheless, there are significant important, differences which can be related to differences in function. In, particular, the centres of the four-helix bundles contain distinctive, groups of hydrophilic residues which have been associated with ferroxidase, activity in H chains and enhanced stability in L chains. L chains contain, a group of glutamates associated with mineralisation within the iron, storage cavity of the protein.
About this StructureAbout this Structure
1AEW is a Single protein structure of sequence from Equus caballus with as ligand. The following page contains interesting information on the relation of 1AEW with [Ferritin and Transferrin]. Known structural/functional Sites: , , and . Full crystallographic information is available from OCA.
ReferenceReference
Comparison of the three-dimensional structures of recombinant human H and horse L ferritins at high resolution., Hempstead PD, Yewdall SJ, Fernie AR, Lawson DM, Artymiuk PJ, Rice DW, Ford GC, Harrison PM, J Mol Biol. 1997 May 2;268(2):424-48. PMID:9159481
Page seeded by OCA on Sun Feb 3 09:30:06 2008