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3ttd
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 3ttd is ON HOLD Authors: Petkun, S., Shi, R., Li, Y., Cygler, M. Description: Crystal structure of E. coli HypF with AMP-CPP and carbamoyl phosphat...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of E. coli HypF with AMP-CPP and carbamoyl phosphate== | |
| + | <StructureSection load='3ttd' size='340' side='right'caption='[[3ttd]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <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> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</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> | ||
| + | <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> | ||
| + | == Function == | ||
| + | [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] | ||
| - | + | ==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]] | |
| - | + | __TOC__ | |
| + | </StructureSection> | ||
| + | [[Category: Escherichia coli O157:H7]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Cygler M]] | ||
| + | [[Category: Li Y]] | ||
| + | [[Category: Petkun S]] | ||
| + | [[Category: Shi R]] | ||
Current revision
Crystal structure of E. coli HypF with AMP-CPP and carbamoyl phosphate
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