7l3v: Difference between revisions

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==PEPCK MMQX structure 120ms post-mixing with oxaloacetic acid==
==PEPCK MMQX structure 120ms post-mixing with oxaloacetic acid==
<StructureSection load='7l3v' size='340' side='right'caption='[[7l3v]]' scene=''>
<StructureSection load='7l3v' size='340' side='right'caption='[[7l3v]], [[Resolution|resolution]] 1.98&Aring;' 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=7L3V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7L3V FirstGlance]. <br>
<table><tr><td colspan='2'>[[7l3v]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7L3V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7L3V FirstGlance]. <br>
</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=7l3v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7l3v OCA], [https://pdbe.org/7l3v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7l3v RCSB], [https://www.ebi.ac.uk/pdbsum/7l3v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7l3v ProSAT]</span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.98&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO2:CARBON+DIOXIDE'>CO2</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=PEP:PHOSPHOENOLPYRUVATE'>PEP</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=7l3v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7l3v OCA], [https://pdbe.org/7l3v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7l3v RCSB], [https://www.ebi.ac.uk/pdbsum/7l3v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7l3v ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PCKGC_RAT PCKGC_RAT] Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic pathway that produces glucose from lactate and other precursors derived from the citric acid cycle.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Time-resolved crystallography of biomolecules in action has advanced rapidly as methods for serial crystallography have improved, but the large number of crystals and the complex experimental infrastructure that are required remain serious obstacles to its widespread application. Here, millisecond mix-and-quench crystallography (MMQX) has been developed, which yields millisecond time-resolved data using far fewer crystals and routine remote synchrotron data collection. To demonstrate the capabilities of MMQX, the conversion of oxaloacetic acid to phosphoenolpyruvate by phosphoenolpyruvate carboxy-kinase (PEPCK) is observed with a time resolution of 40 ms. By lowering the entry barrier to time-resolved crystallography, MMQX should enable a broad expansion in structural studies of protein dynamics.
Millisecond mix-and-quench crystallography (MMQX) enables time-resolved studies of PEPCK with remote data collection.,Clinger JA, Moreau DW, McLeod MJ, Holyoak T, Thorne RE IUCrJ. 2021 Aug 4;8(Pt 5):784-792. doi: 10.1107/S2052252521007053. eCollection, 2021 Sep 1. PMID:34584739<ref>PMID:34584739</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7l3v" style="background-color:#fffaf0;"></div>
==See Also==
*[[Phosphoenolpyruvate carboxykinase 3D structures|Phosphoenolpyruvate carboxykinase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Rattus norvegicus]]
[[Category: Clinger JA]]
[[Category: Clinger JA]]
[[Category: Holyoak T]]
[[Category: Holyoak T]]

Latest revision as of 18:37, 18 October 2023

PEPCK MMQX structure 120ms post-mixing with oxaloacetic acidPEPCK MMQX structure 120ms post-mixing with oxaloacetic acid

Structural highlights

7l3v is a 1 chain structure with sequence from Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.98Å
Ligands:, , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PCKGC_RAT Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic pathway that produces glucose from lactate and other precursors derived from the citric acid cycle.

Publication Abstract from PubMed

Time-resolved crystallography of biomolecules in action has advanced rapidly as methods for serial crystallography have improved, but the large number of crystals and the complex experimental infrastructure that are required remain serious obstacles to its widespread application. Here, millisecond mix-and-quench crystallography (MMQX) has been developed, which yields millisecond time-resolved data using far fewer crystals and routine remote synchrotron data collection. To demonstrate the capabilities of MMQX, the conversion of oxaloacetic acid to phosphoenolpyruvate by phosphoenolpyruvate carboxy-kinase (PEPCK) is observed with a time resolution of 40 ms. By lowering the entry barrier to time-resolved crystallography, MMQX should enable a broad expansion in structural studies of protein dynamics.

Millisecond mix-and-quench crystallography (MMQX) enables time-resolved studies of PEPCK with remote data collection.,Clinger JA, Moreau DW, McLeod MJ, Holyoak T, Thorne RE IUCrJ. 2021 Aug 4;8(Pt 5):784-792. doi: 10.1107/S2052252521007053. eCollection, 2021 Sep 1. PMID:34584739[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Clinger JA, Moreau DW, McLeod MJ, Holyoak T, Thorne RE. Millisecond mix-and-quench crystallography (MMQX) enables time-resolved studies of PEPCK with remote data collection. IUCrJ. 2021 Aug 4;8(Pt 5):784-792. PMID:34584739 doi:10.1107/S2052252521007053

7l3v, resolution 1.98Å

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OCA