2i6r: Difference between revisions

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[[Image:2i6r.png|left|200px]]


{{STRUCTURE_2i6r| PDB=2i6r | SCENE= }}
==Crystal structure of E. coli HypE, a hydrogenase maturation protein==
<StructureSection load='2i6r' size='340' side='right'caption='[[2i6r]], [[Resolution|resolution]] 2.51&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2i6r]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_O157:H7 Escherichia coli O157:H7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2I6R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2I6R FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.51&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2i6r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i6r OCA], [https://pdbe.org/2i6r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2i6r RCSB], [https://www.ebi.ac.uk/pdbsum/2i6r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2i6r ProSAT], [https://www.topsan.org/Proteins/BSGI/2i6r TOPSAN]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/HYPE_ECOLI HYPE_ECOLI] Involved in the maturation of [NiFe] hydrogenases. Along with HypF, it catalyzes the synthesis of the CN ligands of the active site iron of [NiFe]-hydrogenases. HypE catalyzes the ATP-dependent dehydration of the carboxamido group attached to its C-terminal cysteine to a cyano group (PubMed:12586941, PubMed:15291820). The cyano group is then transferred from HypE to the HypC-HypD complex or the HybG-HypD complex (PubMed:15504408).<ref>PMID:12586941</ref> <ref>PMID:15291820</ref> <ref>PMID:15504408</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/i6/2i6r_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </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=2i6r ConSurf].
<div style="clear:both"></div>


===Crystal structure of E. coli HypE, a hydrogenase maturation protein===
==See Also==
 
*[[HypA%2C HypB%2C HypC%2C HypD%2C HypE and HypF 3D structures|HypA%2C HypB%2C HypC%2C HypD%2C HypE and HypF 3D structures]]
{{ABSTRACT_PUBMED_18065529}}
== References ==
 
<references/>
==About this Structure==
__TOC__
[[2i6r]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_o157:h7 Escherichia coli o157:h7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2I6R OCA].
</StructureSection>
 
[[Category: Escherichia coli O157:H7]]
==Reference==
[[Category: Large Structures]]
<ref group="xtra">PMID:018065529</ref><ref group="xtra">PMID:017706667</ref><references group="xtra"/>
[[Category: Cygler M]]
[[Category: Escherichia coli o157:h7]]
[[Category: Iannuzzi P]]
[[Category: BSGI, Montreal-Kingston Bacterial Structural Genomics Initiative.]]
[[Category: Matte A]]
[[Category: Cygler, M.]]
[[Category: Proteau A]]
[[Category: Iannuzzi, P.]]
[[Category: Rangarajan ES]]
[[Category: Matte, A.]]
[[Category: Proteau, A.]]
[[Category: Rangarajan, E S.]]
[[Category: Bsgi]]
[[Category: Hydrogenase maturation protein]]
[[Category: Hype]]
[[Category: Montreal-kingston bacterial structural genomics initiative]]
[[Category: Structural genomic]]
[[Category: Unknown function]]

Latest revision as of 12:01, 21 February 2024

Crystal structure of E. coli HypE, a hydrogenase maturation proteinCrystal structure of E. coli HypE, a hydrogenase maturation protein

Structural highlights

2i6r is a 4 chain structure with sequence from Escherichia coli O157:H7. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.51Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

HYPE_ECOLI Involved in the maturation of [NiFe] hydrogenases. Along with HypF, it catalyzes the synthesis of the CN ligands of the active site iron of [NiFe]-hydrogenases. HypE catalyzes the ATP-dependent dehydration of the carboxamido group attached to its C-terminal cysteine to a cyano group (PubMed:12586941, PubMed:15291820). The cyano group is then transferred from HypE to the HypC-HypD complex or the HybG-HypD complex (PubMed:15504408).[1] [2] [3]

Evolutionary Conservation

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

See Also

References

  1. ↑ Reissmann S, Hochleitner E, Wang H, Paschos A, Lottspeich F, Glass RS, Böck A. Taming of a poison: biosynthesis of the NiFe-hydrogenase cyanide ligands. Science. 2003 Feb 14;299(5609):1067-70. PMID:12586941 doi:10.1126/science.1080972
  2. ↑ Blokesch M, Paschos A, Bauer A, Reissmann S, Drapal N, Bock A. Analysis of the transcarbamoylation-dehydration reaction catalyzed by the hydrogenase maturation proteins HypF and HypE. Eur J Biochem. 2004 Aug;271(16):3428-36. PMID:15291820 doi:http://dx.doi.org/10.1111/j.1432-1033.2004.04280.x
  3. ↑ Blokesch M, Albracht SP, Matzanke BF, Drapal NM, Jacobi A, Bock A. The complex between hydrogenase-maturation proteins HypC and HypD is an intermediate in the supply of cyanide to the active site iron of [NiFe]-hydrogenases. J Mol Biol. 2004 Nov 12;344(1):155-67. PMID:15504408 doi:http://dx.doi.org/10.1016/j.jmb.2004.09.040

2i6r, resolution 2.51Å

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