4qcc: Difference between revisions

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==Structure of a cube-shaped, highly porous protein cage designed by fusing symmetric oligomeric domains==
==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]] 7.08&Aring;' scene=''>
<StructureSection load='4qcc' size='340' side='right'caption='[[4qcc]], [[Resolution|resolution]] 7.08&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4qcc]] is a 2 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QCC FirstGlance]. <br>
<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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/2-dehydro-3-deoxy-6-phosphogalactonate_aldolase 2-dehydro-3-deoxy-6-phosphogalactonate aldolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.21 4.1.2.21] </span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 7.078&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4qcc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qcc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4qcc RCSB], [http://www.ebi.ac.uk/pdbsum/4qcc PDBsum]</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=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>
</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__
__TOC__
</StructureSection>
</StructureSection>
[[Category: 2-dehydro-3-deoxy-6-phosphogalactonate aldolase]]
[[Category: Escherichia coli]]
[[Category: Lai, Y T]]
[[Category: Large Structures]]
[[Category: Yeates, T O]]
[[Category: Lai Y-T]]
[[Category: Bionanotechnology]]
[[Category: Yeates TO]]
[[Category: Lyase]]
[[Category: Porous biomaterial]]
[[Category: Protein design]]
[[Category: Self-assembly]]
[[Category: Structural protein]]
[[Category: Symmetry]]

Latest revision as of 15:45, 1 March 2024

Structure of a cube-shaped, highly porous protein cage designed by fusing symmetric oligomeric domainsStructure of a cube-shaped, highly porous protein cage designed by fusing symmetric oligomeric domains

Structural highlights

4qcc is a 2 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 7.078Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.[1] [2] FKBA_ECOLI PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.

See Also

References

  1. Deacon J, Cooper RA. D-Galactonate utilisation by enteric bacteria. The catabolic pathway in Escherichia coli. FEBS Lett. 1977 May 15;77(2):201-5. PMID:324806
  2. Walters MJ, Srikannathasan V, McEwan AR, Naismith JH, Fierke CA, Toone EJ. Characterization and crystal structure of Escherichia coli KDPGal aldolase. Bioorg Med Chem. 2008 Jan 15;16(2):710-20. Epub 2007 Oct 18. PMID:17981470 doi:10.1016/j.bmc.2007.10.043

4qcc, resolution 7.08Å

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