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< | ==Inter-subunit signaling in GSAM== | ||
<StructureSection load='2hp2' size='340' side='right'caption='[[2hp2]], [[Resolution|resolution]] 2.70Å' scene=''> | |||
You may change the | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2hp2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Anacystis_nidulans Anacystis nidulans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HP2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HP2 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HOZ:(4S)-4,5-DIAMINOPENTANOIC+ACID'>HOZ</scene>, <scene name='pdbligand=KE4:(4R)-5-AMINO-4-[({3-HYDROXY-2-METHYL-5-[(PHOSPHONOOXY)METHYL]PYRIDIN-4-YL}METHYL)AMINO]PENTANOIC+ACID'>KE4</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2hoy|2hoy]], [[2hoz|2hoz]], [[2hp1|2hp1]]</div></td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hemL, gsa ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=269084 Anacystis nidulans])</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Glutamate-1-semialdehyde_2,1-aminomutase Glutamate-1-semialdehyde 2,1-aminomutase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.3.8 5.4.3.8] </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=2hp2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hp2 OCA], [https://pdbe.org/2hp2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hp2 RCSB], [https://www.ebi.ac.uk/pdbsum/2hp2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hp2 ProSAT]</span></td></tr> | |||
</table> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hp/2hp2_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2hp2 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Enzymes are highly dynamic and tightly controlled systems. However, allosteric communication linked to catalytic turnover is poorly understood. We have performed an integrated approach to trap several catalytic intermediates in the alpha2-dimeric key enzyme of chlorophyll biosynthesis, glutamate-1-semialdehyde aminomutase. Our data reveal an active-site "gating loop," which undergoes a dramatic conformational change during catalysis, that is simultaneously open in one subunit and closed in the other. This loop movement requires a beta-sheet-to-alpha-helix transition to assume the closed conformation, thus facilitating transport of substrate toward, and concomitantly forming, an integral part of the active site. The accompanying intersubunit cross-talk, which controls negative cooperativity between the allosteric pair, was explored at the atomic level. The central elements of the communication triad are the cofactor bound to different catalytic intermediates, the interface helix, and the gating loop. Together, they form a molecular switch in which the cofactor acts as a central signal transmitter linking the subunit interface with the gating loop. | |||
Intersubunit signaling in glutamate-1-semialdehyde-aminomutase.,Stetefeld J, Jenny M, Burkhard P Proc Natl Acad Sci U S A. 2006 Sep 12;103(37):13688-93. Epub 2006 Sep 5. PMID:16954186<ref>PMID:16954186</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2hp2" style="background-color:#fffaf0;"></div> | |||
== | ==See Also== | ||
*[[Aminomutase 3D structures|Aminomutase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Anacystis nidulans]] | |||
[[Category: Glutamate-1-semialdehyde 2,1-aminomutase]] | [[Category: Glutamate-1-semialdehyde 2,1-aminomutase]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Stetefeld, J]] | |||
[[Category: Stetefeld, J | |||
[[Category: Inter-subunit signaling]] | [[Category: Inter-subunit signaling]] | ||
[[Category: Isomerase]] | |||
Latest revision as of 10:19, 24 March 2021
Inter-subunit signaling in GSAMInter-subunit signaling in GSAM
Structural highlights
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 PubMedEnzymes are highly dynamic and tightly controlled systems. However, allosteric communication linked to catalytic turnover is poorly understood. We have performed an integrated approach to trap several catalytic intermediates in the alpha2-dimeric key enzyme of chlorophyll biosynthesis, glutamate-1-semialdehyde aminomutase. Our data reveal an active-site "gating loop," which undergoes a dramatic conformational change during catalysis, that is simultaneously open in one subunit and closed in the other. This loop movement requires a beta-sheet-to-alpha-helix transition to assume the closed conformation, thus facilitating transport of substrate toward, and concomitantly forming, an integral part of the active site. The accompanying intersubunit cross-talk, which controls negative cooperativity between the allosteric pair, was explored at the atomic level. The central elements of the communication triad are the cofactor bound to different catalytic intermediates, the interface helix, and the gating loop. Together, they form a molecular switch in which the cofactor acts as a central signal transmitter linking the subunit interface with the gating loop. Intersubunit signaling in glutamate-1-semialdehyde-aminomutase.,Stetefeld J, Jenny M, Burkhard P Proc Natl Acad Sci U S A. 2006 Sep 12;103(37):13688-93. Epub 2006 Sep 5. PMID:16954186[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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