2hmy

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[[Image:2hmy.gif|left|200px]]
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{{Structure
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|PDB= 2hmy |SIZE=350|CAPTION= <scene name='initialview01'>2hmy</scene>, resolution 2.61&Aring;
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The line below this paragraph, containing "STRUCTURE_2hmy", creates the "Structure Box" on the page.
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|LIGAND= <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Deleted_entry Deleted entry], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.73 2.1.1.73] </span>
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{{STRUCTURE_2hmy| PDB=2hmy | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2hmy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hmy OCA], [http://www.ebi.ac.uk/pdbsum/2hmy PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2hmy RCSB]</span>
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'''BINARY COMPLEX OF HHAI METHYLTRANSFERASE WITH ADOMET FORMED IN THE PRESENCE OF A SHORT NONPSECIFIC DNA OLIGONUCLEOTIDE'''
'''BINARY COMPLEX OF HHAI METHYLTRANSFERASE WITH ADOMET FORMED IN THE PRESENCE OF A SHORT NONPSECIFIC DNA OLIGONUCLEOTIDE'''
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[[Category: Roberts, R J.]]
[[Category: Roberts, R J.]]
[[Category: Zhang, X.]]
[[Category: Zhang, X.]]
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[[Category: transferase (methyltransferase)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 06:28:37 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:32:34 2008''
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Revision as of 03:28, 4 May 2008

Template:STRUCTURE 2hmy

BINARY COMPLEX OF HHAI METHYLTRANSFERASE WITH ADOMET FORMED IN THE PRESENCE OF A SHORT NONPSECIFIC DNA OLIGONUCLEOTIDE


Overview

We have determined a structure for a complex formed between HhaI methyltransferase (M.HhaI) and S-adenosyl-L-methionine (AdoMet) in the presence of a non-specific short oligonucleotide. M.HhaI binds to the non-specific short oligonucleotides in solution. Although no DNA is incorporated in the crystal, AdoMet binds in a primed orientation, identical with that observed in the ternary complex of the enzyme, cognate DNA, and AdoMet or S-adenosyl-L-homocysteine (AdoHcy). This orientation differs from the previously observed unprimed orientation in the M.HhaI-AdoMet binary complex, where the S+-CH3 unit of AdoMet is protected by a favorable cation-pi interaction with Trp41. The structure suggests that the presence of DNA can guide AdoMet into the primed orientation. These results shed new light on the proposed ordered mechanism of binding and explains the stable association between AdoMet and M.HhaI.

About this Structure

2HMY is a Single protein structure of sequence from Haemophilus haemolyticus. Full crystallographic information is available from OCA.

Reference

Structure of a binary complex of HhaI methyltransferase with S-adenosyl-L-methionine formed in the presence of a short non-specific DNA oligonucleotide., O'Gara M, Zhang X, Roberts RJ, Cheng X, J Mol Biol. 1999 Mar 26;287(2):201-9. PMID:10080885 Page seeded by OCA on Sun May 4 06:28:37 2008

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