2f00

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[[Image:2f00.jpg|left|200px]]<br /><applet load="2f00" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2f00.jpg|left|200px]]
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caption="2f00, resolution 2.5&Aring;" />
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'''Escherichia coli MurC'''<br />
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{{Structure
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|PDB= 2f00 |SIZE=350|CAPTION= <scene name='initialview01'>2f00</scene>, resolution 2.5&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM ION'>MG</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/UDP-N-acetylmuramate--L-alanine_ligase UDP-N-acetylmuramate--L-alanine ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.2.8 6.3.2.8]
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|GENE= murC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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}}
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'''Escherichia coli MurC'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2F00 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=MG:'>MG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/UDP-N-acetylmuramate--L-alanine_ligase UDP-N-acetylmuramate--L-alanine ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.2.8 6.3.2.8] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F00 OCA].
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2F00 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F00 OCA].
==Reference==
==Reference==
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Structure of Escherichia coli UDP-N-acetylmuramoyl:L-alanine ligase (MurC)., Deva T, Baker EN, Squire CJ, Smith CA, Acta Crystallogr D Biol Crystallogr. 2006 Dec;62(Pt 12):1466-74. Epub 2006, Nov 23. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17139082 17139082]
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Structure of Escherichia coli UDP-N-acetylmuramoyl:L-alanine ligase (MurC)., Deva T, Baker EN, Squire CJ, Smith CA, Acta Crystallogr D Biol Crystallogr. 2006 Dec;62(Pt 12):1466-74. Epub 2006, Nov 23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17139082 17139082]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: bacterial cell wall]]
[[Category: bacterial cell wall]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:16:19 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:46:27 2008''

Revision as of 14:46, 20 March 2008


PDB ID 2f00

Drag the structure with the mouse to rotate
, resolution 2.5Å
Ligands:
Gene: murC (Escherichia coli)
Activity: UDP-N-acetylmuramate--L-alanine ligase, with EC number 6.3.2.8
Coordinates: save as pdb, mmCIF, xml



Escherichia coli MurC


Overview

The bacterial cell wall provides essential protection from the external environment and confers strength and rigidity to counteract internal osmotic pressure. Without this layer the cell would be easily ruptured and it is for this reason that biosynthetic pathways leading to the formation of peptidoglycan have for many years been a prime target for effective antibiotics. Central to this pathway are four similar ligase enzymes which add peptide groups to glycan moieties. As part of a program to better understand the structure-function relationships in these four enzymes, the crystal structure of Escherichia coli UDP-N-acetylmuramoyl:L-alanine ligase (MurC) has been determined to 2.6 A resolution. The structure was solved by multiwavelength anomalous diffraction methods from a single selenomethionine-substituted crystal and refined to a crystallographic R factor of 0.212 (R(free) = 0.259). The enzyme has a modular multi-domain structure very similar to those of other members of the mur family of ATP-dependent amide-bond ligases. Detailed comparison of these four enzymes shows that considerable conformational changes are possible. These changes, together with the recruitment of two different N-terminal domains, allow this family of enzymes to bind a substrate which is identical at one end and at the other has the growing peptide tail which will ultimately become part of the rigid bacterial cell wall. Comparison of the E. coli and Haemophilus influenzae structures and analysis of the sequences of known MurC enzymes indicate the presence of a ;dimerization' motif in almost 50% of the MurC enzymes and points to a highly conserved loop in domain 3 that may play a key role in amino-acid ligand specificity.

About this Structure

2F00 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Structure of Escherichia coli UDP-N-acetylmuramoyl:L-alanine ligase (MurC)., Deva T, Baker EN, Squire CJ, Smith CA, Acta Crystallogr D Biol Crystallogr. 2006 Dec;62(Pt 12):1466-74. Epub 2006, Nov 23. PMID:17139082

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