1e5s: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older edit
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,615 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,615 edits
No edit summary
 
(13 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1e5s.gif|left|200px]]<br /><applet load="1e5s" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1e5s, resolution 2.40&Aring;" />
'''PROLINE 3-HYDROXYLASE (TYPE II)-IRON FORM'''<br />


==Overview==
==Proline 3-hydroxylase (type II) - Iron form==
Iron (II)/2-oxoglutarate (2-OG)-dependent oxygenases catalyse oxidative reactions in a range of metabolic processes including the hydroxylation of proline and lysine residues during the post-translational modification of collagen. 2-OG oxygenases commonly require ascorbate for full activity. In the vitamin C deficient disease, scurvy, reduced activity of 2-OG oxygenases results in impaired formation of collagen. Here we report the crystal structure of bacterial proline 3-hydroxylase from Streptomyces sp., an enzyme which hydroxylates proline at position 3, the first of a 2-OG oxygenase catalysing oxidation of a free alpha-amino acid. Structures were obtained for the enzyme in the absence of iron (to 2.3A resolution, R=20.2%, Rfree=25.3%) and that complexed to iron (II) (to 2.4A resolution, R=19.8%, Rfree=22.6%). The structure contains conserved motifs present in other 2-OG oxygenases including a 'jelly roll' beta strand core and residues binding iron and 2-oxoglutarate, consistent with divergent evolution within the extended family. The structure differs significantly from many other 2-OG oxygenases in possessing a discrete C-terminal helical domain. Analysis of the structure suggests a model for proline binding and a mechanism for uncoupling of proline and 2-OG turnover.
<StructureSection load='1e5s' size='340' side='right'caption='[[1e5s]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[1e5s]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_sp._TH1 Streptomyces sp. TH1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E5S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E5S FirstGlance]. <br>
1E5S is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_sp. Streptomyces sp.] with <scene name='pdbligand=FE2:'>FE2</scene> and <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E5S OCA].  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
 
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
==Reference==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1e5s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e5s OCA], [https://pdbe.org/1e5s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e5s RCSB], [https://www.ebi.ac.uk/pdbsum/1e5s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e5s ProSAT]</span></td></tr>
Structure of proline 3-hydroxylase. Evolution of the family of 2-oxoglutarate dependent oxygenases., Clifton IJ, Hsueh LC, Baldwin JE, Harlos K, Schofield CJ, Eur J Biochem. 2001 Dec;268(24):6625-36. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11737217 11737217]
</table>
[[Category: Single protein]]
== Function ==
[[Category: Streptomyces sp.]]
[https://www.uniprot.org/uniprot/P3H2_STRSQ P3H2_STRSQ] Dioxygenase that catalyzes the 2-oxoglutarate-dependent selective hydroxylation of free L-proline to cis-3-hydroxy-L-proline (cis-3-Hyp).[PDB:1E5R]
[[Category: Baldwin, J E.]]
== Evolutionary Conservation ==
[[Category: Clifton, I J.]]
[[Image:Consurf_key_small.gif|200px|right]]
[[Category: Harlos, K.]]
Check<jmol>
[[Category: Hsueh, L C.]]
  <jmolCheckbox>
[[Category: Schofield, C J.]]
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e5/1e5s_consurf.spt"</scriptWhenChecked>
[[Category: FE2]]
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
[[Category: SO4]]
    <text>to colour the structure by Evolutionary Conservation</text>
[[Category: 2-oxoglutarate dependent oxygenase]]
  </jmolCheckbox>
 
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1e5s ConSurf].
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:24:06 2008''
<div style="clear:both"></div>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptomyces sp. TH1]]
[[Category: Baldwin JE]]
[[Category: Clifton IJ]]
[[Category: Harlos K]]
[[Category: Hsueh LC]]
[[Category: Schofield CJ]]

Latest revision as of 09:58, 20 March 2024

Proline 3-hydroxylase (type II) - Iron form

1e5s, resolution 2.40Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1e5s&oldid=4107818"