6x2e: Difference between revisions
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==Crystal Structure of Chlamydia trachomatis mixed (apo/holo) Glyceraldehyde 3-phosphate dehydrogenase== | ==Crystal Structure of Chlamydia trachomatis mixed (apo/holo) Glyceraldehyde 3-phosphate dehydrogenase== | ||
<StructureSection load='6x2e' size='340' side='right'caption='[[6x2e]]' scene=''> | <StructureSection load='6x2e' size='340' side='right'caption='[[6x2e]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6X2E OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6X2E FirstGlance]. <br> | <table><tr><td colspan='2'>[[6x2e]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Chltr Chltr]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6X2E OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6X2E FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6x2e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6x2e OCA], [http://pdbe.org/6x2e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6x2e RCSB], [http://www.ebi.ac.uk/pdbsum/6x2e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6x2e ProSAT]</span></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr> | ||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CME:S,S-(2-HYDROXYETHYL)THIOCYSTEINE'>CME</scene>, <scene name='pdbligand=SNC:S-NITROSO-CYSTEINE'>SNC</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;'>[[6wyc|6wyc]]</div></td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">gap, gapA, CT_505 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=272561 CHLTR])</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glyceraldehyde-3-phosphate_dehydrogenase_(phosphorylating) Glyceraldehyde-3-phosphate dehydrogenase (phosphorylating)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.1.12 1.2.1.12] </span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6x2e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6x2e OCA], [http://pdbe.org/6x2e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6x2e RCSB], [http://www.ebi.ac.uk/pdbsum/6x2e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6x2e ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/G3P_CHLTR G3P_CHLTR]] Catalyzes the oxidative phosphorylation of glyceraldehyde 3-phosphate (G3P) to 1,3-bisphosphoglycerate (BPG) using the cofactor NAD. The first reaction step involves the formation of a hemiacetal intermediate between G3P and a cysteine residue, and this hemiacetal intermediate is then oxidized to a thioester, with concomitant reduction of NAD to NADH. The reduced NADH is then exchanged with the second NAD, and the thioester is attacked by a nucleophilic inorganic phosphate to produce BPG.[UniProtKB:P00362] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Glyceraldehyde 3-phosphate dehydrogenase (GAPDH) is an evolutionarily conserved essential enzyme in the glycolytic pathway. GAPDH is also involved in a wide spectrum of non-catalytic cellular 'moonlighting' functions. Bacterial surface-associated GAPDHs engage in many host interactions that aid in colonization, pathogenesis, and virulence. We have structurally and functionally characterized the recombinant GAPDH of the obligate intracellular bacteria Chlamydia trachomatis, the leading cause of sexually transmitted bacterial and ocular infections. Contrary to earlier speculations, recent data confirm the presence of glucose-catabolizing enzymes including GAPDH in both stages of the biphasic life cycle of the bacterium. The high-resolution crystal structure described here provides a close-up view of the enzyme's active site and surface topology and reveals two chemically modified cysteine residues. Moreover, we show for the first time that purified C. trachomatis GAPDH binds to human plasminogen and plasmin. Based on the versatility of GAPDH's functions, data presented here emphasize the need for investigating the Chlamydiae GAPDH's involvement in biological functions beyond energy metabolism. | |||
Chlamydia trachomatis glyceraldehyde 3-phosphate dehydrogenase: Enzyme kinetics, high-resolution crystal structure, and plasminogen binding.,Schormann N, Campos J, Motamed R, Hayden KL, Gould JR, Green TJ, Senkovich O, Banerjee S, Ulett GC, Chattopadhyay D Protein Sci. 2020 Oct 15. doi: 10.1002/pro.3975. PMID:33058314<ref>PMID:33058314</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6x2e" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Chltr]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Chattopadhyay D]] | [[Category: Chattopadhyay, D]] | ||
[[Category: Schormann N]] | [[Category: Schormann, N]] | ||
[[Category: Chlamydia]] | |||
[[Category: Gapdh]] | |||
[[Category: Glycolysis]] | |||
[[Category: Nad]] | |||
[[Category: Oxidoreductase]] | |||
Revision as of 11:13, 2 December 2020
Crystal Structure of Chlamydia trachomatis mixed (apo/holo) Glyceraldehyde 3-phosphate dehydrogenaseCrystal Structure of Chlamydia trachomatis mixed (apo/holo) Glyceraldehyde 3-phosphate dehydrogenase
Structural highlights
Function[G3P_CHLTR] Catalyzes the oxidative phosphorylation of glyceraldehyde 3-phosphate (G3P) to 1,3-bisphosphoglycerate (BPG) using the cofactor NAD. The first reaction step involves the formation of a hemiacetal intermediate between G3P and a cysteine residue, and this hemiacetal intermediate is then oxidized to a thioester, with concomitant reduction of NAD to NADH. The reduced NADH is then exchanged with the second NAD, and the thioester is attacked by a nucleophilic inorganic phosphate to produce BPG.[UniProtKB:P00362] Publication Abstract from PubMedGlyceraldehyde 3-phosphate dehydrogenase (GAPDH) is an evolutionarily conserved essential enzyme in the glycolytic pathway. GAPDH is also involved in a wide spectrum of non-catalytic cellular 'moonlighting' functions. Bacterial surface-associated GAPDHs engage in many host interactions that aid in colonization, pathogenesis, and virulence. We have structurally and functionally characterized the recombinant GAPDH of the obligate intracellular bacteria Chlamydia trachomatis, the leading cause of sexually transmitted bacterial and ocular infections. Contrary to earlier speculations, recent data confirm the presence of glucose-catabolizing enzymes including GAPDH in both stages of the biphasic life cycle of the bacterium. The high-resolution crystal structure described here provides a close-up view of the enzyme's active site and surface topology and reveals two chemically modified cysteine residues. Moreover, we show for the first time that purified C. trachomatis GAPDH binds to human plasminogen and plasmin. Based on the versatility of GAPDH's functions, data presented here emphasize the need for investigating the Chlamydiae GAPDH's involvement in biological functions beyond energy metabolism. Chlamydia trachomatis glyceraldehyde 3-phosphate dehydrogenase: Enzyme kinetics, high-resolution crystal structure, and plasminogen binding.,Schormann N, Campos J, Motamed R, Hayden KL, Gould JR, Green TJ, Senkovich O, Banerjee S, Ulett GC, Chattopadhyay D Protein Sci. 2020 Oct 15. doi: 10.1002/pro.3975. PMID:33058314[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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