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| - | [[Image:1m80.gif|left|200px]] | + | #REDIRECT [[3m10]] This PDB entry is obsolete and replaced by 3m10 |
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| - | {{Structure
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| - | |PDB= 1m80 |SIZE=350|CAPTION= <scene name='initialview01'>1m80</scene>, resolution 2.35Å
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| - | |SITE=
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| - | |LIGAND=
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| - | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Arginine_kinase Arginine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.3.3 2.7.3.3] </span>
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| - | |GENE=
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| - | |DOMAIN=
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| - | |RELATEDENTRY=[[1bg0|1BG0]]
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| - | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1m80 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m80 OCA], [http://www.ebi.ac.uk/pdbsum/1m80 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1m80 RCSB]</span>
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| - | }}
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| - | '''SUBSTRATE FREE FORM OF ARGININE KINASE'''
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| - | ==Overview==
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| - | Arginine kinase (AK) is a member of the guanidino kinase family that plays an important role in buffering ATP concentration in cells with high and fluctuating energy demands. The AK specifically catalyzes the reversible phosphoryl transfer between ATP and arginine. We have determined the crystal structure of AK from the horseshoe crab (Limulus polyphemus) in its open (substrate-free) form. The final model has been refined at 2.35 A with a final R of 22.3% (R(free) = 23.7%). The structure of the open form is compared to the previously determined structure of the transition state analog complex in the closed form. Classically, the protein would be considered two domain, but dynamic domain (DynDom) analysis shows that most of the differences between the two structures can be considered as the motion between four rigid groups of nonsequential residues. ATP binds near a cluster of positively charged residues of a fixed dynamic domain. The other three dynamic domains close the active site with separate hinge rotations relative to the fixed domain. Several residues of key importance for the induced motion are conserved within the phosphagen kinase family, including creatine kinase. Substantial conformational changes are induced in different parts of the enzyme as intimate interactions are formed with both substrates. Thus, although induced fit occurs in a number of phosphoryl transfer enzymes, the conformational changes in phosphagen kinases appear to be more complicated than in prior examples.
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| - | ==About this Structure==
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| - | 1M80 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Limulus_polyphemus Limulus polyphemus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M80 OCA].
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| - | ==Reference==
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| - | Induced fit in guanidino kinases--comparison of substrate-free and transition state analog structures of arginine kinase., Yousef MS, Clark SA, Pruett PK, Somasundaram T, Ellington WR, Chapman MS, Protein Sci. 2003 Jan;12(1):103-11. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12493833 12493833]
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| - | [[Category: Arginine kinase]]
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| - | [[Category: Limulus polyphemus]]
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| - | [[Category: Single protein]]
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| - | [[Category: Chapman, M S.]]
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| - | [[Category: Clark, S A.]]
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| - | [[Category: Ellington, W R.]]
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| - | [[Category: Pruett, P K.]]
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| - | [[Category: Somasundaram, T.]]
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| - | [[Category: Yousef, M S.]]
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| - | [[Category: arginine kinase]]
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| - | [[Category: creatine kinase]]
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| - | [[Category: guanidino kina structure]]
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| - | [[Category: induced fit]]
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| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:12:37 2008''
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