7yzk: Difference between revisions
New page: '''Unreleased structure''' The entry 7yzk is ON HOLD Authors: Description: Category: Unreleased Structures |
No edit summary |
||
| (3 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
==Structure of Mycobacterium tuberculosis adenylyl cyclase Rv1625c / Cya== | |||
<StructureSection load='7yzk' size='340' side='right'caption='[[7yzk]], [[Resolution|resolution]] 3.57Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7yzk]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis] and [https://en.wikipedia.org/wiki/Vicugna_pacos Vicugna pacos]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7YZK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7YZK FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=ONM:3-O-(N-METHYLANTHRANILOYL)-GUANOSINE-5-TRIPHOSPHATE'>ONM</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=7yzk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7yzk OCA], [https://pdbe.org/7yzk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7yzk RCSB], [https://www.ebi.ac.uk/pdbsum/7yzk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7yzk ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[https://www.uniprot.org/uniprot/A0A5R1ZCG6_MYCTX A0A5R1ZCG6_MYCTX]] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Mycobacterium tuberculosis adenylyl cyclase (AC) Rv1625c / Cya is an evolutionary ancestor of the mammalian membrane ACs and a model system for studies of their structure and function. Although the vital role of ACs in cellular signaling is well established, the function of their transmembrane (TM) regions remains unknown. Here we describe the cryo-EM structure of Cya bound to a stabilizing nanobody at 3.6 A resolution. The TM helices 1-5 form a structurally conserved domain that facilitates the assembly of the helical and catalytic domains. The TM region contains discrete pockets accessible from the extracellular and cytosolic side of the membrane. Neutralization of the negatively charged extracellular pocket Ex1 destabilizes the cytosolic helical domain and reduces the catalytic activity of the enzyme. The TM domain acts as a functional component of Cya, guiding the assembly of the catalytic domain and providing the means for direct regulation of catalytic activity in response to extracellular ligands. | |||
Structure of Mycobacterium tuberculosis Cya, an evolutionary ancestor of the mammalian membrane adenylyl cyclases.,Mehta V, Khanppnavar B, Schuster D, Kantarci I, Vercellino I, Kosturanova A, Iype T, Stefanic S, Picotti P, Korkhov VM Elife. 2022 Aug 18;11. pii: 77032. doi: 10.7554/eLife.77032. PMID:35980026<ref>PMID:35980026</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 7yzk" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Mycobacterium tuberculosis]] | |||
[[Category: Vicugna pacos]] | |||
[[Category: Khanppnavar B]] | |||
[[Category: Korkhov VM]] | |||
[[Category: Mehta V]] | |||
Latest revision as of 22:34, 7 September 2022
Structure of Mycobacterium tuberculosis adenylyl cyclase Rv1625c / CyaStructure of Mycobacterium tuberculosis adenylyl cyclase Rv1625c / Cya
Structural highlights
FunctionPublication Abstract from PubMedMycobacterium tuberculosis adenylyl cyclase (AC) Rv1625c / Cya is an evolutionary ancestor of the mammalian membrane ACs and a model system for studies of their structure and function. Although the vital role of ACs in cellular signaling is well established, the function of their transmembrane (TM) regions remains unknown. Here we describe the cryo-EM structure of Cya bound to a stabilizing nanobody at 3.6 A resolution. The TM helices 1-5 form a structurally conserved domain that facilitates the assembly of the helical and catalytic domains. The TM region contains discrete pockets accessible from the extracellular and cytosolic side of the membrane. Neutralization of the negatively charged extracellular pocket Ex1 destabilizes the cytosolic helical domain and reduces the catalytic activity of the enzyme. The TM domain acts as a functional component of Cya, guiding the assembly of the catalytic domain and providing the means for direct regulation of catalytic activity in response to extracellular ligands. Structure of Mycobacterium tuberculosis Cya, an evolutionary ancestor of the mammalian membrane adenylyl cyclases.,Mehta V, Khanppnavar B, Schuster D, Kantarci I, Vercellino I, Kosturanova A, Iype T, Stefanic S, Picotti P, Korkhov VM Elife. 2022 Aug 18;11. pii: 77032. doi: 10.7554/eLife.77032. PMID:35980026[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||