3mch: Difference between revisions
No edit summary |
No edit summary |
||
| (3 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
== | ==Crystal structure of the molybdopterin biosynthesis enzyme MoaB (TTHA0341) from thermus theromophilus HB8== | ||
[[3mch]] is a 3 chain structure with sequence from [ | <StructureSection load='3mch' size='340' side='right'caption='[[3mch]], [[Resolution|resolution]] 1.64Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3mch]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB8 Thermus thermophilus HB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MCH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MCH 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]] 1.64Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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=3mch FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mch OCA], [https://pdbe.org/3mch PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mch RCSB], [https://www.ebi.ac.uk/pdbsum/3mch PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mch ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q5SLF2_THET8 Q5SLF2_THET8] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Molybdenum-cofactor (Moco) biosynthesis is an evolutionarily conserved pathway in almost all kingdoms of life, including humans. Two proteins, MogA and MoeA, catalyze the last step of this pathway in bacteria, whereas a single two-domain protein carries out catalysis in eukaryotes. Here, three crystal structures of the Moco-biosynthesis protein MogA from the two thermophilic organisms Thermus thermophilus (TtMogA; 1.64 A resolution, space group P2(1)) and Aquifex aeolicus (AaMogA; 1.70 A resolution, space group P2(1) and 1.90 A resolution, space group P1) have been determined. The functional roles and the residues involved in oligomerization of the protein molecules have been identified based on a comparative analysis of these structures with those of homologous proteins. Furthermore, functional roles have been proposed for the N- and C-terminal residues. In addition, a possible protein-protein complex of MogA and MoeA has been proposed and the residues involved in protein-protein interactions are discussed. Several invariant water molecules and those present at the subunit interfaces have been identified and their possible structural and/or functional roles are described in brief. In addition, molecular-dynamics and docking studies with several small molecules (including the substrate and the product) have been carried out in order to estimate their binding affinities towards AaMogA and TtMogA. The results obtained are further compared with those obtained for homologous eukaryotic proteins. | |||
Crystal structures, dynamics and functional implications of molybdenum-cofactor biosynthesis protein MogA from two thermophilic organisms.,Kanaujia SP, Jeyakanthan J, Shinkai A, Kuramitsu S, Yokoyama S, Sekar K Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Jan 1;67(Pt, 1):2-16. Epub 2010 Dec 21. PMID:21206014<ref>PMID:21206014</ref> | |||
<ref | |||
[[Category: Thermus thermophilus]] | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
[[Category: Baba | </div> | ||
[[Category: Ebihara | <div class="pdbe-citations 3mch" style="background-color:#fffaf0;"></div> | ||
[[Category: Jeyakanthan | == References == | ||
[[Category: Kanaujia | <references/> | ||
[[Category: Kuramitsu | __TOC__ | ||
</StructureSection> | |||
[[Category: Sekar | [[Category: Large Structures]] | ||
[[Category: Shinkai | [[Category: Thermus thermophilus HB8]] | ||
[[Category: Shiro | [[Category: Baba S]] | ||
[[Category: Yokoyama | [[Category: Ebihara A]] | ||
[[Category: Jeyakanthan J]] | |||
[[Category: Kanaujia SP]] | |||
[[Category: Kuramitsu S]] | |||
[[Category: Sekar K]] | |||
[[Category: Shinkai A]] | |||
[[Category: Shiro Y]] | |||
[[Category: Yokoyama S]] | |||
Latest revision as of 19:31, 1 November 2023
Crystal structure of the molybdopterin biosynthesis enzyme MoaB (TTHA0341) from thermus theromophilus HB8Crystal structure of the molybdopterin biosynthesis enzyme MoaB (TTHA0341) from thermus theromophilus HB8
Structural highlights
FunctionPublication Abstract from PubMedMolybdenum-cofactor (Moco) biosynthesis is an evolutionarily conserved pathway in almost all kingdoms of life, including humans. Two proteins, MogA and MoeA, catalyze the last step of this pathway in bacteria, whereas a single two-domain protein carries out catalysis in eukaryotes. Here, three crystal structures of the Moco-biosynthesis protein MogA from the two thermophilic organisms Thermus thermophilus (TtMogA; 1.64 A resolution, space group P2(1)) and Aquifex aeolicus (AaMogA; 1.70 A resolution, space group P2(1) and 1.90 A resolution, space group P1) have been determined. The functional roles and the residues involved in oligomerization of the protein molecules have been identified based on a comparative analysis of these structures with those of homologous proteins. Furthermore, functional roles have been proposed for the N- and C-terminal residues. In addition, a possible protein-protein complex of MogA and MoeA has been proposed and the residues involved in protein-protein interactions are discussed. Several invariant water molecules and those present at the subunit interfaces have been identified and their possible structural and/or functional roles are described in brief. In addition, molecular-dynamics and docking studies with several small molecules (including the substrate and the product) have been carried out in order to estimate their binding affinities towards AaMogA and TtMogA. The results obtained are further compared with those obtained for homologous eukaryotic proteins. Crystal structures, dynamics and functional implications of molybdenum-cofactor biosynthesis protein MogA from two thermophilic organisms.,Kanaujia SP, Jeyakanthan J, Shinkai A, Kuramitsu S, Yokoyama S, Sekar K Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Jan 1;67(Pt, 1):2-16. Epub 2010 Dec 21. PMID:21206014[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||||