6th8: Difference between revisions

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==Reconstructing the Origins of the HemD-like fold==
==Reconstructing the Origins of the HemD-like fold==
<StructureSection load='6th8' size='340' side='right'caption='[[6th8]], [[NMR_Ensembles_of_Models | 21 NMR models]]' scene=''>
<StructureSection load='6th8' size='340' side='right'caption='[[6th8]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6th8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"flavobacterium_thermophilum"_yoshida_and_oshima_1971 "flavobacterium thermophilum" yoshida and oshima 1971]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TH8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6TH8 FirstGlance]. <br>
<table><tr><td colspan='2'>[[6th8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TH8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6TH8 FirstGlance]. <br>
</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=6th8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6th8 OCA], [http://pdbe.org/6th8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6th8 RCSB], [http://www.ebi.ac.uk/pdbsum/6th8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6th8 ProSAT]</span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=6th8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6th8 OCA], [https://pdbe.org/6th8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6th8 RCSB], [https://www.ebi.ac.uk/pdbsum/6th8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6th8 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/HEM4_PSEAE HEM4_PSEAE] Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III.
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Flavobacterium thermophilum yoshida and oshima 1971]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Chaubey, M]]
[[Category: Thermus thermophilus]]
[[Category: Coles, M]]
[[Category: Chaubey M]]
[[Category: Hocker, B]]
[[Category: Coles M]]
[[Category: Toledo-Patino, S]]
[[Category: Hocker B]]
[[Category: Flavodoxin-like fold]]
[[Category: Toledo-Patino S]]
[[Category: Flavoprotein]]
[[Category: Hemd-like fold]]
[[Category: Protein design]]

Latest revision as of 09:09, 19 June 2024

Reconstructing the Origins of the HemD-like foldReconstructing the Origins of the HemD-like fold

Structural highlights

6th8 is a 1 chain structure with sequence from Thermus thermophilus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

HEM4_PSEAE Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III.

Publication Abstract from PubMed

Evolutionary processes that led to the emergence of structured protein domains left footprints in the sequences of modern proteins. We searched for such hints employing state-of-the-art sequence analysis and found evidence that the HemD-like fold emerged from the flavodoxin-like fold through segment swap and gene duplication. To verify this hypothesis, we reverted these evolutionary steps experimentally, constructing a HemD-half that resulted in a protein with the canonical flavodoxin-like architecture. These results of fold reconstruction from the sequence of a different fold strongly support our hypothesis of common ancestry. It further illustrates the plasticity of modern proteins to form new folded proteins.

Reconstructing the Remote Origins of a Fold Singleton from a Flavodoxin-Like Ancestor.,Toledo-Patino S, Chaubey M, Coles M, Hocker B Biochemistry. 2019 Nov 20. doi: 10.1021/acs.biochem.9b00900. PMID:31724394[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Toledo-Patino S, Chaubey M, Coles M, Hocker B. Reconstructing the Remote Origins of a Fold Singleton from a Flavodoxin-Like Ancestor. Biochemistry. 2019 Nov 20. doi: 10.1021/acs.biochem.9b00900. PMID:31724394 doi:http://dx.doi.org/10.1021/acs.biochem.9b00900
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