4qcc
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of a cube-shaped, highly porous protein cage designed by fusing symmetric oligomeric domains== | |
| + | <StructureSection load='4qcc' size='340' side='right'caption='[[4qcc]], [[Resolution|resolution]] 7.08Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4qcc]] is a 2 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=4QCC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4QCC 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]] 7.078Å</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=4qcc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qcc OCA], [https://pdbe.org/4qcc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qcc RCSB], [https://www.ebi.ac.uk/pdbsum/4qcc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qcc ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/DGOA_ECOLI DGOA_ECOLI] Involved in the degradation of galactose via the DeLey-Doudoroff pathway. Catalyzes the reversible, stereospecific retro-aldol cleavage of 2-keto-3-deoxy-6-phosphogalactonate (KDPGal) to pyruvate and D-glyceraldehyde-3-phosphate. In the synthetic direction, it catalyzes the addition of pyruvate to electrophilic aldehydes with re-facial selectivity. It can use a limited number of aldehyde substrates, including D-glyceraldehyde-3-phosphate (natural substrate), D-glyceraldehyde, glycolaldehyde, 2-pyridinecarboxaldehyde, D-ribose, D-erythrose and D-threose. It efficiently catalyzes aldol addition only using pyruvate as the nucleophilic component and accepts both stereochemical configurations at C2 of the electrophile.<ref>PMID:324806</ref> <ref>PMID:17981470</ref> [https://www.uniprot.org/uniprot/FKBA_ECOLI FKBA_ECOLI] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. | ||
| - | + | ==See Also== | |
| - | + | *[[Aldolase 3D structures|Aldolase 3D structures]] | |
| - | + | == References == | |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Escherichia coli]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Lai Y-T]] | ||
| + | [[Category: Yeates TO]] | ||
Current revision
Structure of a cube-shaped, highly porous protein cage designed by fusing symmetric oligomeric domains
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