3ttd

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<StructureSection load='3ttd' size='340' side='right'caption='[[3ttd]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='3ttd' size='340' side='right'caption='[[3ttd]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3ttd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Eco57 Eco57]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TTD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TTD FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3ttd]] is a 1 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=3TTD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TTD FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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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]] 2.2&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3tsp|3tsp]], [[3tsq|3tsq]], [[3tsu|3tsu]], [[3ttc|3ttc]], [[3ttf|3ttf]]</div></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=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ECs3568, hypf ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83334 ECO57])</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=3ttd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ttd OCA], [https://pdbe.org/3ttd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ttd RCSB], [https://www.ebi.ac.uk/pdbsum/3ttd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ttd ProSAT]</span></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=3ttd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ttd OCA], [https://pdbe.org/3ttd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ttd RCSB], [https://www.ebi.ac.uk/pdbsum/3ttd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ttd ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/A0A0H3JHT3_ECO57 A0A0H3JHT3_ECO57] Involved in the maturation of [NiFe] hydrogenases. Along with HypE, it catalyzes the synthesis of the CN ligands of the active site iron of [NiFe]-hydrogenases. HypF 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.[PIRNR:PIRNR006256]
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[NiFe]-hydrogenases are multimeric proteins. The large subunit contains the NiFe(CN)(2)CO bimetallic active center and the small subunit contains Fe-S clusters. Biosynthesis and assembly of the NiFe(CN)(2)CO active center requires six Hyp accessory proteins. The synthesis of the CN(-) ligands is catalyzed by the combined actions of HypF and HypE using carbamoylphosphate as a substrate. We report the structure of Escherichia coli HypF(92-750) lacking the N-terminal acylphosphatase domain. HypF(92-750) comprises the novel Zn-finger domain, the nucleotide-binding YrdC-like domain, and the Kae1-like universal domain, also binding a nucleotide and a Zn(2+) ion. The two nucleotide-binding sites are sequestered in an internal cavity, facing each other and separated by approximately 14 A. The YrdC-like domain converts carbamoyl moiety to a carbamoyl adenylate intermediate, which is channeled to the Kae1-like domain. Mutations within either nucleotide-binding site compromise hydrogenase maturation but do not affect the carbamoylphosphate phosphatase activity.
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Structure of Hydrogenase Maturation Protein HypF with Reaction Intermediates Shows Two Active Sites.,Petkun S, Shi R, Li Y, Asinas A, Munger C, Zhang L, Waclawek M, Soboh B, Sawers RG, Cygler M Structure. 2011 Dec 7;19(12):1773-83. PMID:22153500<ref>PMID:22153500</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3ttd" style="background-color:#fffaf0;"></div>
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==See Also==
==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]]
*[[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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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Eco57]]
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[[Category: Escherichia coli O157:H7]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Cygler, M]]
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[[Category: Cygler M]]
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[[Category: Li, Y]]
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[[Category: Li Y]]
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[[Category: Petkun, S]]
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[[Category: Petkun S]]
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[[Category: Shi, R]]
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[[Category: Shi R]]
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[[Category: Hydrogenase maturation factor]]
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[[Category: Hype]]
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[[Category: Nucleotide binding]]
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[[Category: Transferase]]
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[[Category: Zn finger]]
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Current revision

Crystal structure of E. coli HypF with AMP-CPP and carbamoyl phosphate

PDB ID 3ttd

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OCA

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