3lzc: Difference between revisions

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[[Image:3lzc.png|left|200px]]


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==Crystal structure of Dph2 from Pyrococcus horikoshii==
The line below this paragraph, containing "STRUCTURE_3lzc", creates the "Structure Box" on the page.
<StructureSection load='3lzc' size='340' side='right'caption='[[3lzc]], [[Resolution|resolution]] 2.26&Aring;' scene=''>
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== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[3lzc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_horikoshii Pyrococcus horikoshii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LZC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LZC FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.261&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3lzc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lzc OCA], [https://pdbe.org/3lzc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3lzc RCSB], [https://www.ebi.ac.uk/pdbsum/3lzc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3lzc ProSAT]</span></td></tr>
{{STRUCTURE_3lzc|  PDB=3lzc  |  SCENE=  }}
</table>
 
== Function ==
===Crystal structure of Dph2 from Pyrococcus horikoshii===
[https://www.uniprot.org/uniprot/DPH2_PYRHO DPH2_PYRHO] Catalyzes the first step of diphthamide biosynthesis, i.e. the transfer of the 3-amino-3-carboxypropyl group from S-adenosyl-L-methionine (SAM) to the C2 position of the imidazole ring of the target histidine residue in translation elongation factor 2 (EF-2).<ref>PMID:20559380</ref>  
 
== Evolutionary Conservation ==
 
[[Image:Consurf_key_small.gif|200px|right]]
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==About this Structure==
</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=3lzc ConSurf].
3LZC is a 2 chains structure with sequences from [http://en.wikipedia.org/wiki/Pyrococcus_horikoshii Pyrococcus horikoshii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LZC OCA].  
<div style="clear:both"></div>
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:20559380</ref><references group="xtra"/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pyrococcus horikoshii]]
[[Category: Pyrococcus horikoshii]]
[[Category: Dzikovski, B.]]
[[Category: Dzikovski B]]
[[Category: Ealick, S E.]]
[[Category: Ealick SE]]
[[Category: Freed, J.]]
[[Category: Freed J]]
[[Category: Koralewski, R M.]]
[[Category: Koralewski RM]]
[[Category: Krebs, C.]]
[[Category: Krebs C]]
[[Category: Lee, M.]]
[[Category: Lee M]]
[[Category: Lin, H.]]
[[Category: Lin H]]
[[Category: Torelli, A T.]]
[[Category: Torelli AT]]
[[Category: Wang, E.]]
[[Category: Wang E]]
[[Category: Zhang, Y.]]
[[Category: Zhang Y]]
[[Category: Zhu, X.]]
[[Category: Zhu X]]
[[Category: Biosynthetic protein]]
[[Category: Diphthamide biosynthesis]]
[[Category: Gene triplication]]
[[Category: Radical sam enzyme]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 14 15:53:00 2010''

Latest revision as of 13:23, 21 February 2024

Crystal structure of Dph2 from Pyrococcus horikoshiiCrystal structure of Dph2 from Pyrococcus horikoshii

Structural highlights

3lzc is a 2 chain structure with sequence from Pyrococcus horikoshii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.261Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

DPH2_PYRHO Catalyzes the first step of diphthamide biosynthesis, i.e. the transfer of the 3-amino-3-carboxypropyl group from S-adenosyl-L-methionine (SAM) to the C2 position of the imidazole ring of the target histidine residue in translation elongation factor 2 (EF-2).[1]

Evolutionary Conservation

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

References

  1. Zhang Y, Zhu X, Torelli AT, Lee M, Dzikovski B, Koralewski RM, Wang E, Freed J, Krebs C, Ealick SE, Lin H. Diphthamide biosynthesis requires an organic radical generated by an iron-sulphur enzyme. Nature. 2010 Jun 17;465(7300):891-6. PMID:20559380 doi:10.1038/nature09138

3lzc, resolution 2.26Å

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