2b3l

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{{Seed}}
 
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[[Image:2b3l.png|left|200px]]
 
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==Crystal structure of type I human methionine aminopeptidase in the apo form==
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The line below this paragraph, containing "STRUCTURE_2b3l", creates the "Structure Box" on the page.
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<StructureSection load='2b3l' size='340' side='right'caption='[[2b3l]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2b3l]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B3L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2B3L FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr>
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{{STRUCTURE_2b3l| PDB=2b3l | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2b3l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b3l OCA], [https://pdbe.org/2b3l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2b3l RCSB], [https://www.ebi.ac.uk/pdbsum/2b3l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2b3l ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/MAP11_HUMAN MAP11_HUMAN] Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Required for normal progression through the cell cycle.[HAMAP-Rule:MF_03174]<ref>PMID:16274222</ref> <ref>PMID:17114291</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/b3/2b3l_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=2b3l ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Determination of the crystal structure of human MetAP1 makes it possible, for the first time, to compare the structures of a Type I and a Type II methionine aminopeptidase (MetAP) from the same organism. Comparison of the Type I enzyme with the previously reported complex of ovalicin with Type II MetAP shows that the active site of the former is reduced in size and would incur steric clashes with the bound inhibitor. This explains why ovalicin and related anti-angiogenesis inhibitors target Type II human MetAP but not Type I. The differences in both size and shape of the active sites between MetAP1 and MetAP2 also help to explain their different substrate specificity. In the presence of excess Co(2+), a third cobalt ion binds in the active site region, explaining why metal ions in excess can be inhibitory. Also, the N-terminal region of the protein contains three distinct Pro-x-x-Pro motifs, supporting the prior suggestion that this region of the protein may participate in binding to the ribosome.
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===Crystal structure of type I human methionine aminopeptidase in the apo form===
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Structural basis for the functional differences between type I and type II human methionine aminopeptidases.,Addlagatta A, Hu X, Liu JO, Matthews BW Biochemistry. 2005 Nov 15;44(45):14741-9. PMID:16274222<ref>PMID:16274222</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_16274222}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2b3l" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 16274222 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_16274222}}
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__TOC__
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</StructureSection>
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==About this Structure==
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2B3L is a 1 chain 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=2B3L OCA].
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==Reference==
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<ref group="xtra">PMID:16274222</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Methionyl aminopeptidase]]
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[[Category: Large Structures]]
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[[Category: Addlagatta, A.]]
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[[Category: Addlagatta A]]
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[[Category: Hu, X.]]
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[[Category: Hu X]]
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[[Category: Liu, J O.]]
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[[Category: Liu JO]]
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[[Category: Matthews, B W.]]
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[[Category: Matthews BW]]
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[[Category: Human]]
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[[Category: Hydrolase]]
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[[Category: Metalloprotease]]
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[[Category: Methionine aminopeptidase]]
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[[Category: Pitabread fold]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 12:53:29 2009''
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Current revision

Crystal structure of type I human methionine aminopeptidase in the apo form

PDB ID 2b3l

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