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<StructureSection load='1fwk' size='340' side='right'caption='[[1fwk]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
<StructureSection load='1fwk' size='340' side='right'caption='[[1fwk]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1fwk]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43067 Atcc 43067]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FWK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FWK FirstGlance]. <br>
<table><tr><td colspan='2'>[[1fwk]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FWK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FWK FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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]] 2.1&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1fwl|1fwl]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Homoserine_kinase Homoserine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.39 2.7.1.39] </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=1fwk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fwk OCA], [https://pdbe.org/1fwk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fwk RCSB], [https://www.ebi.ac.uk/pdbsum/1fwk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fwk ProSAT]</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=1fwk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fwk OCA], [http://pdbe.org/1fwk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1fwk RCSB], [http://www.ebi.ac.uk/pdbsum/1fwk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1fwk ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/KHSE_METJA KHSE_METJA]] Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate (By similarity).  
[https://www.uniprot.org/uniprot/KHSE_METJA KHSE_METJA] Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate (By similarity).
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=1fwk ConSurf].
</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=1fwk ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
BACKGROUND: Homoserine kinase (HSK) catalyzes an important step in the threonine biosynthesis pathway. It belongs to a large yet unique class of small metabolite kinases, the GHMP kinase superfamily. Members in the GHMP superfamily participate in several essential metabolic pathways, such as amino acid biosynthesis, galactose metabolism, and the mevalonate pathway. RESULTS: The crystal structure of HSK and its complex with ADP reveal a novel nucleotide binding fold. The N-terminal domain contains an unusual left-handed betaalphabeta unit, while the C-terminal domain has a central alpha-beta plait fold with an insertion of four helices. The phosphate binding loop in HSK is distinct from the classical P loops found in many ATP/GTP binding proteins. The bound ADP molecule adopts a rare syn conformation and is in the opposite orientation from those bound to the P loop-containing proteins. Inspection of the substrate binding cavity indicates several amino acid residues that are likely to be involved in substrate binding and catalysis. CONCLUSIONS: The crystal structure of HSK is the first representative in the GHMP superfamily to have determined structure. It provides insight into the structure and nucleotide binding mechanism of not only the HSK family but also a variety of enzymes in the GHMP superfamily. Such enzymes include galactokinases, mevalonate kinases, phosphomevalonate kinases, mevalonate pyrophosphate decarboxylases, and several proteins of yet unknown functions.
Structure and mechanism of homoserine kinase: prototype for the GHMP kinase superfamily.,Zhou T, Daugherty M, Grishin NV, Osterman AL, Zhang H Structure. 2000 Dec 15;8(12):1247-57. PMID:11188689<ref>PMID:11188689</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1fwk" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 43067]]
[[Category: Homoserine kinase]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Daugherty, M]]
[[Category: Methanocaldococcus jannaschii]]
[[Category: Grishin, N V]]
[[Category: Daugherty M]]
[[Category: Osterman, A L]]
[[Category: Grishin NV]]
[[Category: Zhang, H]]
[[Category: Osterman AL]]
[[Category: Zhou, T]]
[[Category: Zhang H]]
[[Category: Kinase]]
[[Category: Zhou T]]
[[Category: Transferase]]

Latest revision as of 10:19, 7 February 2024

CRYSTAL STRUCTURE OF HOMOSERINE KINASE COMPLEXED WITH ADPCRYSTAL STRUCTURE OF HOMOSERINE KINASE COMPLEXED WITH ADP

Structural highlights

1fwk is a 4 chain structure with sequence from Methanocaldococcus jannaschii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.1Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

KHSE_METJA Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate (By similarity).

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

1fwk, resolution 2.10Å

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