2hp2: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2hp2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Synechococcus_elongatus Synechococcus elongatus]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2HP2 FirstGlance]. <br> | <table><tr><td colspan='2'>[[2hp2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Synechococcus_elongatus Synechococcus elongatus]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2HP2 FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2hoy|2hoy]], [[2hoz|2hoz]], [[2hp1|2hp1]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2hoy|2hoy]], [[2hoz|2hoz]], [[2hp1|2hp1]]</td></tr> | ||
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hemL, gsa ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=32046 Synechococcus elongatus])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hemL, gsa ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=32046 Synechococcus elongatus])</td></tr> | ||
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutamate-1-semialdehyde_2,1-aminomutase Glutamate-1-semialdehyde 2,1-aminomutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.3.8 5.4.3.8] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutamate-1-semialdehyde_2,1-aminomutase Glutamate-1-semialdehyde 2,1-aminomutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.3.8 5.4.3.8] </span></td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2hp2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hp2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2hp2 RCSB], [http://www.ebi.ac.uk/pdbsum/2hp2 PDBsum]</span></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=2hp2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hp2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2hp2 RCSB], [http://www.ebi.ac.uk/pdbsum/2hp2 PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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[[Category: Glutamate-1-semialdehyde 2,1-aminomutase]] | [[Category: Glutamate-1-semialdehyde 2,1-aminomutase]] | ||
[[Category: Synechococcus elongatus]] | [[Category: Synechococcus elongatus]] | ||
[[Category: Stetefeld, J | [[Category: Stetefeld, J]] | ||
[[Category: Inter-subunit signaling]] | [[Category: Inter-subunit signaling]] | ||
[[Category: Isomerase]] | [[Category: Isomerase]] | ||
Revision as of 12:17, 16 January 2015
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. References |
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