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1gxt

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[[Image:1gxt.gif|left|200px]]<br />
 
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<applet load="1gxt" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1gxt, resolution 1.27&Aring;" />
 
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'''HYDROGENASE MATURATION PROTEIN HYPF "ACYLPHOSPHATASE-LIKE" N-TERMINAL DOMAIN (HYPF-ACP) IN COMPLEX WITH SULFATE'''<br />
 
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==Overview==
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==Hydrogenase Maturation Protein HypF "acylphosphatase-like" N-terminal domain (HypF-ACP) in complex with Sulfate==
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[NiFe]-hydrogenases require a set of complementary and regulatory proteins, for correct folding and maturation processes. One of the essential, regulatory proteins, HypF (82kDa) contains a N-terminal acylphosphatase, (ACT)-like domain, a sequence motif shared with enzymes catalyzing, O-carbamoylation, and two zinc finger motifs similar to those found in the, DnaJ chaperone. The HypF acylphosphatase domain is thought to support the, conversion of carbamoylphosphate into CO and CN(-), promoting coordination, of these ligands to the hydrogenase metal cluster. It has been shown, recently that the HypF N-terminal domain can aggregate in vitro to yield, fibrils matching those formed by proteins linked to amyloid diseases. The, 1.27A resolution HypF acylphosphatase domain crystal structure ... [[http://ispc.weizmann.ac.il/pmbin/getpm?12206761 (full description)]]
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<StructureSection load='1gxt' size='340' side='right'caption='[[1gxt]], [[Resolution|resolution]] 1.27&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1gxt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GXT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GXT 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]] 1.27&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></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=1gxt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gxt OCA], [https://pdbe.org/1gxt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gxt RCSB], [https://www.ebi.ac.uk/pdbsum/1gxt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gxt ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/HYPF_ECOLI HYPF_ECOLI] Along with HypE, it catalyzes the synthesis of the CN ligands of the active site iron of [NiFe]-hydrogenases using carbamoylphosphate as a substrate. It functions as a carbamoyl transferase using carbamoylphosphate as a substrate and transferring the carboxamido moiety in an ATP-dependent reaction to the thiolate of the C-terminal cysteine of HypE yielding a protein-S-carboxamide.<ref>PMID:8661925</ref> <ref>PMID:12377778</ref> <ref>PMID:15291820</ref> <ref>PMID:15504408</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gx/1gxt_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1gxt ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1GXT is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]] with CL, SO4 and TRS as [[http://en.wikipedia.org/wiki/ligands ligands]]. Structure known Active Site: CLA. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GXT OCA]].
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*[[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]]
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== References ==
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==Reference==
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<references/>
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Crystal structure and anion binding in the prokaryotic hydrogenase maturation factor HypF acylphosphatase-like domain., Rosano C, Zuccotti S, Bucciantini M, Stefani M, Ramponi G, Bolognesi M, J Mol Biol. 2002 Aug 30;321(5):785-96. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12206761 12206761]
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__TOC__
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</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Bolognesi, M.]]
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[[Category: Bolognesi M]]
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[[Category: Bucciantini, M.]]
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[[Category: Bucciantini M]]
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[[Category: Ramponi, G.]]
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[[Category: Ramponi G]]
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[[Category: Rosano, C.]]
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[[Category: Rosano C]]
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[[Category: Stefani, M.]]
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[[Category: Stefani M]]
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[[Category: Zuccotti, S.]]
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[[Category: Zuccotti S]]
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[[Category: CL]]
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[[Category: SO4]]
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[[Category: TRS]]
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[[Category: acylphosphatases]]
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[[Category: complete proteome]]
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[[Category: fibril formation]]
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[[Category: hydrogenase maturations]]
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[[Category: zinc-finger]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 11:57:48 2007''
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Current revision

Hydrogenase Maturation Protein HypF "acylphosphatase-like" N-terminal domain (HypF-ACP) in complex with Sulfate

PDB ID 1gxt

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