5awe: Difference between revisions
New page: '''Unreleased structure''' The entry 5awe is ON HOLD Authors: Nakabayashi, M., Shibata, N., Kanagawa, M., Nakagawa, N., Kuramitsu, S., Higuchi, Y. Description: Crystal structure of a h... |
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The | ==Crystal structure of a hypothetical protein, TTHA0829 from Thermus thermophilus HB8, composed of cystathionine-beta-synthase (CBS) and aspartate-kinase chorismate-mutase tyrA (ACT) domains== | ||
<StructureSection load='5awe' size='340' side='right'caption='[[5awe]], [[Resolution|resolution]] 2.45Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5awe]] is a 1 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=5AWE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5AWE 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]] 2.45Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=5awe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5awe OCA], [https://pdbe.org/5awe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5awe RCSB], [https://www.ebi.ac.uk/pdbsum/5awe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5awe ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q5SK23_THET8 Q5SK23_THET8] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
TTHA0829 from Thermus thermophilus HB8 has a molecular mass of 22,754 Da and is composed of 210 amino acid residues. The expression of TTHA0829 is remarkably elevated in the latter half of logarithmic growth phase. TTHA0829 can form either a tetrameric or dimeric structure, and main-chain folding provides an N-terminal cystathionine-beta-synthase (CBS) domain and a C-terminal aspartate-kinase chorismate-mutase tyrA (ACT) domain. Both CBS and ACT are regulatory domains to which a small ligand molecule can bind. The CBS domain is found in proteins from organisms belonging to all kingdoms and is observed frequently as two or four tandem copies. This domain is considered as a small intracellular module with a regulatory function and is typically found adjacent to the active (or functional) site of several enzymes and integral membrane proteins. The ACT domain comprises four beta-strands and two alpha-helices in a betaalphabetabetaalphabeta motif typical of intracellular small molecule binding domains that help control metabolism, solute transport and signal transduction. We discuss the possible role of TTHA0829 based on its structure and expression pattern. The results imply that TTHA0829 acts as a cell-stress sensor or a metabolite acceptor. | |||
Crystal structure of a hypothetical protein, TTHA0829 from Thermus thermophilus HB8, composed of cystathionine-beta-synthase (CBS) and aspartate-kinase chorismate-mutase tyrA (ACT) domains.,Nakabayashi M, Shibata N, Ishido-Nakai E, Kanagawa M, Iio Y, Komori H, Ueda Y, Nakagawa N, Kuramitsu S, Higuchi Y Extremophiles. 2016 May;20(3):275-82. doi: 10.1007/s00792-016-0817-y. Epub 2016, Mar 3. PMID:26936147<ref>PMID:26936147</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5awe" style="background-color:#fffaf0;"></div> | ||
[[Category: Higuchi | == References == | ||
[[Category: Kanagawa | <references/> | ||
[[Category: Kuramitsu | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Thermus thermophilus HB8]] | |||
[[Category: Higuchi Y]] | |||
[[Category: Kanagawa M]] | |||
[[Category: Kuramitsu S]] | |||
[[Category: Nakabayashi M]] | |||
[[Category: Nakagawa N]] | |||
[[Category: Shibata N]] | |||
Latest revision as of 11:35, 9 October 2024
Crystal structure of a hypothetical protein, TTHA0829 from Thermus thermophilus HB8, composed of cystathionine-beta-synthase (CBS) and aspartate-kinase chorismate-mutase tyrA (ACT) domainsCrystal structure of a hypothetical protein, TTHA0829 from Thermus thermophilus HB8, composed of cystathionine-beta-synthase (CBS) and aspartate-kinase chorismate-mutase tyrA (ACT) domains
Structural highlights
FunctionPublication Abstract from PubMedTTHA0829 from Thermus thermophilus HB8 has a molecular mass of 22,754 Da and is composed of 210 amino acid residues. The expression of TTHA0829 is remarkably elevated in the latter half of logarithmic growth phase. TTHA0829 can form either a tetrameric or dimeric structure, and main-chain folding provides an N-terminal cystathionine-beta-synthase (CBS) domain and a C-terminal aspartate-kinase chorismate-mutase tyrA (ACT) domain. Both CBS and ACT are regulatory domains to which a small ligand molecule can bind. The CBS domain is found in proteins from organisms belonging to all kingdoms and is observed frequently as two or four tandem copies. This domain is considered as a small intracellular module with a regulatory function and is typically found adjacent to the active (or functional) site of several enzymes and integral membrane proteins. The ACT domain comprises four beta-strands and two alpha-helices in a betaalphabetabetaalphabeta motif typical of intracellular small molecule binding domains that help control metabolism, solute transport and signal transduction. We discuss the possible role of TTHA0829 based on its structure and expression pattern. The results imply that TTHA0829 acts as a cell-stress sensor or a metabolite acceptor. Crystal structure of a hypothetical protein, TTHA0829 from Thermus thermophilus HB8, composed of cystathionine-beta-synthase (CBS) and aspartate-kinase chorismate-mutase tyrA (ACT) domains.,Nakabayashi M, Shibata N, Ishido-Nakai E, Kanagawa M, Iio Y, Komori H, Ueda Y, Nakagawa N, Kuramitsu S, Higuchi Y Extremophiles. 2016 May;20(3):275-82. doi: 10.1007/s00792-016-0817-y. Epub 2016, Mar 3. PMID:26936147[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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