This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

1rhc

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 10:13, 15 September 2021

F420-dependent secondary alcohol dehydrogenase in complex with an F420-acetone adduct

Structural highlights

1rhc is a 1 chain structure with sequence from Methanoculleus thermophilus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

F(420)-dependent secondary alcohol dehydrogenase (Adf) from methanogenic archaea is a member of the growing bacterial luciferase family which are all TIM barrel enzymes, most of which with an unusual nonprolyl cis peptide bond. We report here on the crystal structure of Adf from Methanoculleus thermophilicus at 1.8 A resolution in complex with a F(420)-acetone adduct. The knowledge of the F(420) binding mode in Adf provides the molecular basis for modeling F(420) and FMN into the other enzymes of the family. A nonprolyl cis peptide bond was identified as an essential part of a bulge that serves as backstop at the Re-face of F(420) to keep it in a bent conformation. The acetone moiety of the F(420)-acetone adduct is positioned at the Si-face of F(420) deeply buried inside the protein. Isopropanol can be reliably modeled and a hydrogen transfer mechanism postulated. His39 and Glu108 can be identified as key players for binding of the acetone or isopropanol oxygens and for catalysis.

Coenzyme binding in F420-dependent secondary alcohol dehydrogenase, a member of the bacterial luciferase family.,Aufhammer SW, Warkentin E, Berk H, Shima S, Thauer RK, Ermler U Structure. 2004 Mar;12(3):361-70. PMID:15016352^[1]

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

References

↑ Aufhammer SW, Warkentin E, Berk H, Shima S, Thauer RK, Ermler U. Coenzyme binding in F420-dependent secondary alcohol dehydrogenase, a member of the bacterial luciferase family. Structure. 2004 Mar;12(3):361-70. PMID:15016352 doi:10.1016/j.str.2004.02.010

1 Structural highlights
2 Evolutionary Conservation
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1rhc"

@@ Line 3: / Line 3: @@
 <StructureSection load='1rhc' size='340' side='right'caption='[[1rhc]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1rhc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Methanoculleus_thermophilus Methanoculleus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RHC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1RHC FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1rhc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanoculleus_thermophilus Methanoculleus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RHC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RHC FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACN:ACETONE'>ACN</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=F42:COENZYME+F420'>F42</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACN:ACETONE'>ACN</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=F42:COENZYME+F420'>F42</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene></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=1rhc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rhc OCA], [http://pdbe.org/1rhc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1rhc RCSB], [http://www.ebi.ac.uk/pdbsum/1rhc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1rhc 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=1rhc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rhc OCA], [https://pdbe.org/1rhc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rhc RCSB], [https://www.ebi.ac.uk/pdbsum/1rhc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rhc ProSAT]</span></td></tr>
 </table>
 == Evolutionary Conservation ==

1rhc

From Proteopedia

Revision as of 10:13, 15 September 2021

F420-dependent secondary alcohol dehydrogenase in complex with an F420-acetone adduct

Structural highlights

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox