2dq5: Difference between revisions

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[[Image:2dq5.jpg|left|200px]]
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[[Image:2dq5.png|left|200px]]


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{{STRUCTURE_2dq5|  PDB=2dq5  |  SCENE=  }}  
{{STRUCTURE_2dq5|  PDB=2dq5  |  SCENE=  }}  


'''solution structure of the Mid1 B Box2 Chc(D/C)C2H2 Zinc-Binding Domain: insights into an evolutionary conserved ring fold'''
===solution structure of the Mid1 B Box2 Chc(D/C)C2H2 Zinc-Binding Domain: insights into an evolutionary conserved ring fold===




==Overview==
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The B-box type 2 domain is a prominent feature of a large and growing family of RING, B-box, coiled-coil (RBCC) domain-containing proteins and is also present in more than 1500 additional proteins. Most proteins usually contain a single B-box2 domain, although some proteins contain tandem domains consisting of both type 1 and type 2 B-boxes, which actually share little sequence similarity. Recently, we determined the solution structure of B-box1 from MID1, a putative E3 ubiquitin ligase that is mutated in X-linked Opitz G/BBB syndrome, and showed that it adopted a betabetaalpha RING-like fold. Here, we report the tertiary structure of the B-box2 (CHC(D/C)C(2)H(2)) domain from MID1 using multidimensional NMR spectroscopy. This MID1 B-box2 domain consists of a short alpha-helix and a structured loop with two short anti-parallel beta-strands and adopts a tertiary structure similar to the B-box1 and RING structures, even though there is minimal primary sequence similarity between these domains. By mutagenesis, ESI-FTICR and ICP mass spectrometry, we show that the B-box2 domain coordinates two zinc atoms with a 'cross-brace' pattern: one by Cys175, His178, Cys195 and Cys198 and the other by Cys187, Asp190, His204, and His207. Interestingly, this is the first case that an aspartic acid is involved in zinc atom coordination in a zinc-finger domain, although aspartic acid has been shown to coordinate non-catalytic zinc in matrix metalloproteinases. In addition, the finding of a Cys195Phe substitution identified in a patient with X-linked Opitz GBBB syndrome supports the importance of proper zinc coordination for the function of the MID1 B-box2 domain. Notably, however, our structure differs from the only other published B-box2 structure, that from XNF7, which was shown to coordinate one zinc atom. Finally, the similarity in tertiary structures of the B-box2, B-box1 and RING domains suggests these domains have evolved from a common ancestor.
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==Disease==
==Disease==
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==About this Structure==
==About this Structure==
2DQ5 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DQ5 OCA].  
2DQ5 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DQ5 OCA].  


==Reference==
==Reference==
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[[Category: Ring like]]
[[Category: Ring like]]
[[Category: Zinc coordination]]
[[Category: Zinc coordination]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 00:57:04 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 02:10:20 2008''

Revision as of 23:10, 27 July 2008

File:2dq5.png

Template:STRUCTURE 2dq5

solution structure of the Mid1 B Box2 Chc(D/C)C2H2 Zinc-Binding Domain: insights into an evolutionary conserved ring fold

Template:ABSTRACT PUBMED 17428496

Disease

Known disease associated with this structure: Opitz G syndrome, type I OMIM:[300552]

About this Structure

2DQ5 is a Single protein structure of sequence from Homo sapiens. Full experimental information is available from OCA.

Reference

Solution structure of the MID1 B-box2 CHC(D/C)C(2)H(2) zinc-binding domain: insights into an evolutionarily conserved RING fold., Massiah MA, Matts JA, Short KM, Simmons BN, Singireddy S, Yi Z, Cox TC, J Mol Biol. 2007 May 25;369(1):1-10. Epub 2007 Mar 15. PMID:17428496

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